12866_2008_642_moesm1_esm.xls… · xls file · web view · 2015-12-11plays a role in assembling...

289
locus_tag replicon a/b- a/c- a/b+ a/c+ b-/c- b-/b+ PSPTO0003 NC_004578.1 NA 0.84312 NA 0.65362 NA NA PSPTO0005 NC_004578.1 NA NA NA 0.50524 NA NA PSPTO0022 NC_004578.1 NA NA NA -0.9353 NA NA PSPTO0023 NC_004578.1 NA NA NA -0.9519 NA NA PSPTO0044 NC_004578.1 NA NA -1.1049 -1.2571 NA NA PSPTO0061 NC_004578.1 NA NA NA -1.565 NA NA PSPTO0062 NC_004578.1 -5.9324 NA -6.2152 NA NA NA PSPTO0064 NC_004578.1 NA NA NA -0.448 NA NA PSPTO0067 NC_004578.1 NA NA 3.84136 3.91 NA NA PSPTO0068 NC_004578.1 NA NA 4.65457 4.69283 NA NA PSPTO0069 NC_004578.1 NA NA 7.1373 6.959 NA 7.46069 PSPTO0072 NC_004578.1 NA 0.29514 NA NA NA NA PSPTO0073 NC_004578.1 NA NA NA NA NA NA PSPTO0075 NC_004578.1 NA 1.10531 NA NA NA NA PSPTO0087 NC_004578.1 NA NA NA -0.3692 NA NA PSPTO0092 NC_004578.1 NA NA NA NA NA NA PSPTO0101 NC_004578.1 NA NA NA -0.9633 NA NA PSPTO0110 NC_004578.1 NA NA NA -1.219 NA NA PSPTO0113 NC_004578.1 NA 0.49722 NA NA NA NA PSPTO0125 NC_004578.1 NA NA NA NA NA NA PSPTO0134 NC_004578.1 NA NA NA -0.3727 NA NA PSPTO0136 NC_004578.1 NA -0.429 NA NA NA NA PSPTO0144 NC_004578.1 NA NA NA -0.4625 NA NA PSPTO0152 NC_004578.1 NA NA NA NA NA NA PSPTO0154 NC_004578.1 NA NA -0.6568 NA NA NA PSPTO0156 NC_004578.1 NA NA -0.4584 0.73851 NA NA PSPTO0165 NC_004578.1 NA NA NA -0.6017 NA NA PSPTO0167 NC_004578.1 NA NA NA NA NA NA PSPTO0203 NC_004578.1 NA -1.3171 NA NA NA NA PSPTO0206 NC_004578.1 NA -0.8625 NA -0.6989 NA NA PSPTO0208 NC_004578.1 NA 0.69937 NA 0.61853 NA NA PSPTO0210 NC_004578.1 NA NA NA 0.85864 NA NA PSPTO0211 NC_004578.1 NA NA NA 0.97247 NA NA PSPTO0217 NC_004578.1 NA NA NA NA NA NA PSPTO0219 NC_004578.1 NA 0.89557 NA 0.82021 NA NA PSPTO0220 NC_004578.1 NA 0.64416 NA 0.78114 NA NA PSPTO0231 NC_004578.1 NA -0.8374 NA -0.8075 NA NA PSPTO0239 NC_004578.1 NA 0.54842 NA NA NA NA PSPTO0279 NC_004578.1 NA NA NA 1.13722 NA NA PSPTO0283 NC_004578.1 NA 3.75692 NA 2.33856 NA NA PSPTO0307 NC_004578.1 NA NA NA 2.64447 NA NA PSPTO0308 NC_004578.1 NA NA NA 1.0803 NA NA PSPTO0309 NC_004578.1 NA NA NA 1.26234 NA NA PSPTO0314 NC_004578.1 NA NA 3.80277 2.45708 NA 4.11759 PSPTO0316 NC_004578.1 NA NA NA NA NA NA PSPTO0322 NC_004578.1 NA 0.5594 NA NA NA NA PSPTO0325 NC_004578.1 NA 0.27627 NA NA NA NA PSPTO0328 NC_004578.1 NA NA NA -0.8486 NA NA PSPTO0330 NC_004578.1 -1.4305 NA -1.5379 1.19139 NA NA PSPTO0351 NC_004578.1 NA NA NA -0.9341 NA NA PSPTO0359 NC_004578.1 NA -0.3568 NA NA NA NA Supplemental Table 1: Differentially regulated genes identified a

Upload: buimien

Post on 23-Apr-2018

225 views

Category:

Documents


1 download

TRANSCRIPT

Page 1: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

locus_tag replicon a/b- a/c- a/b+ a/c+ b-/c-PSPTO0003 NC_004578.1 NA 0.8431209 NA 0.6536205 NAPSPTO0005 NC_004578.1 NA NA NA 0.505242 NAPSPTO0022 NC_004578.1 NA NA NA -0.935258 NAPSPTO0023 NC_004578.1 NA NA NA -0.951915 NAPSPTO0044 NC_004578.1 NA NA -1.104889 -1.25709 NAPSPTO0061 NC_004578.1 NA NA NA -1.564984 NAPSPTO0062 NC_004578.1 -5.932367 NA -6.215231 NA NAPSPTO0064 NC_004578.1 NA NA NA -0.448033 NAPSPTO0067 NC_004578.1 NA NA 3.8413599 3.909999 NAPSPTO0068 NC_004578.1 NA NA 4.6545684 4.6928295 NAPSPTO0069 NC_004578.1 NA NA 7.1372996 6.9590005 NAPSPTO0072 NC_004578.1 NA 0.2951424 NA NA NAPSPTO0073 NC_004578.1 NA NA NA NA NAPSPTO0075 NC_004578.1 NA 1.1053125 NA NA NAPSPTO0087 NC_004578.1 NA NA NA -0.369187 NAPSPTO0092 NC_004578.1 NA NA NA NA NAPSPTO0101 NC_004578.1 NA NA NA -0.963287 NAPSPTO0110 NC_004578.1 NA NA NA -1.218984 NAPSPTO0113 NC_004578.1 NA 0.4972157 NA NA NAPSPTO0125 NC_004578.1 NA NA NA NA NAPSPTO0134 NC_004578.1 NA NA NA -0.37274 NAPSPTO0136 NC_004578.1 NA -0.428994 NA NA NAPSPTO0144 NC_004578.1 NA NA NA -0.462536 NAPSPTO0152 NC_004578.1 NA NA NA NA NAPSPTO0154 NC_004578.1 NA NA -0.656779 NA NAPSPTO0156 NC_004578.1 NA NA -0.458426 0.7385076 NAPSPTO0165 NC_004578.1 NA NA NA -0.601723 NAPSPTO0167 NC_004578.1 NA NA NA NA NAPSPTO0203 NC_004578.1 NA -1.31709 NA NA NAPSPTO0206 NC_004578.1 NA -0.862528 NA -0.698857 NAPSPTO0208 NC_004578.1 NA 0.6993746 NA 0.6185334 NAPSPTO0210 NC_004578.1 NA NA NA 0.8586403 NAPSPTO0211 NC_004578.1 NA NA NA 0.9724669 NAPSPTO0217 NC_004578.1 NA NA NA NA NAPSPTO0219 NC_004578.1 NA 0.8955745 NA 0.8202102 NAPSPTO0220 NC_004578.1 NA 0.6441649 NA 0.7811363 NAPSPTO0231 NC_004578.1 NA -0.837421 NA -0.807538 NAPSPTO0239 NC_004578.1 NA 0.5484198 NA NA NAPSPTO0279 NC_004578.1 NA NA NA 1.1372168 NAPSPTO0283 NC_004578.1 NA 3.7569243 NA 2.3385575 NAPSPTO0307 NC_004578.1 NA NA NA 2.6444655 NAPSPTO0308 NC_004578.1 NA NA NA 1.0802995 NAPSPTO0309 NC_004578.1 NA NA NA 1.2623372 NAPSPTO0314 NC_004578.1 NA NA 3.8027727 2.4570779 NAPSPTO0316 NC_004578.1 NA NA NA NA NAPSPTO0322 NC_004578.1 NA 0.5593973 NA NA NAPSPTO0325 NC_004578.1 NA 0.2762708 NA NA NAPSPTO0328 NC_004578.1 NA NA NA -0.848594 NAPSPTO0330 NC_004578.1 -1.430511 NA -1.537885 1.1913944 NAPSPTO0351 NC_004578.1 NA NA NA -0.934102 NAPSPTO0359 NC_004578.1 NA -0.356776 NA NA NAPSPTO0361 NC_004578.1 NA NA NA NA NAPSPTO0371 NC_004578.1 NA NA NA -0.733963 NAPSPTO0383 NC_004578.1 NA NA NA 0.5958605 NAPSPTO0386 NC_004578.1 NA 0.642277 NA NA NAPSPTO0389 NC_004578.1 NA 0.9066142 NA NA NA

Supplemental Table 1: Differentially regulated genes identified at a p value less than or equal to 0.05 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 2: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO0420 NC_004578.1 NA NA NA -0.511693 NAPSPTO0425 NC_004578.1 NA NA 1.102138 0.8296596 NAPSPTO0426 NC_004578.1 NA NA 1.0670061 0.859924 NAPSPTO0430 NC_004578.1 NA NA NA -0.194794 NAPSPTO0433 NC_004578.1 NA 0.8663837 NA 0.5028522 NAPSPTO0434 NC_004578.1 NA 0.6099881 NA NA NAPSPTO0441 NC_004578.1 NA NA NA 0.1714415 NAPSPTO0448 NC_004578.1 NA NA NA NA NAPSPTO0455 NC_004578.1 NA NA NA -0.703409 NAPSPTO0499 NC_004578.1 NA NA NA -0.65536 NAPSPTO0503 NC_004578.1 NA NA -1.102675 -1.814398 NAPSPTO0509 NC_004578.1 NA 0.6350724 NA NA NAPSPTO0524 NC_004578.1 NA 1.0337622 -1.913905 -1.691704 NAPSPTO0539 NC_004578.1 NA 0.5883879 NA 0.3819594 NAPSPTO0545 NC_004578.1 NA NA NA -1.966044 NAPSPTO0546 NC_004578.1 NA -1.70605 NA -1.156065 NAPSPTO0547 NC_004578.1 NA -1.238183 NA -0.889579 NAPSPTO0549 NC_004578.1 NA 0.5388626 NA 0.7144517 NAPSPTO0550 NC_004578.1 NA 1.1133408 NA NA NAPSPTO0551 NC_004578.1 NA 1.0223871 NA 0.5333087 NAPSPTO0552 NC_004578.1 NA NA NA 0.654005 NAPSPTO0567 NC_004578.1 NA NA NA NA NAPSPTO0568 NC_004578.1 NA NA NA NA NAPSPTO0569 NC_004578.1 NA -0.869586 NA -1.397638 NAPSPTO0570 NC_004578.1 NA -1.328624 NA -1.46596 NAPSPTO0572 NC_004578.1 NA NA NA -0.616448 NAPSPTO0588 NC_004578.1 NA NA -0.583547 -1.015811 NAPSPTO0589 NC_004578.1 NA NA NA -1.196069 NAPSPTO0594 NC_004578.1 NA NA NA -0.412115 NAPSPTO0598 NC_004578.1 NA 1.3766065 NA NA NAPSPTO0602 NC_004578.1 NA NA NA NA NAPSPTO0603 NC_004578.1 NA NA NA -0.894106 NAPSPTO0604 NC_004578.1 NA NA NA NA NAPSPTO0606 NC_004578.1 NA NA NA NA NAPSPTO0609 NC_004578.1 NA 0.3663835 NA NA NAPSPTO0613 NC_004578.1 NA 0.521243 NA 0.3507872 NAPSPTO0614 NC_004578.1 NA 0.4750536 NA NA NAPSPTO0615 NC_004578.1 NA NA NA 0.2556747 NAPSPTO0616 NC_004578.1 NA NA NA 0.2199688 NAPSPTO0617 NC_004578.1 NA NA NA 0.1664693 NAPSPTO0618 NC_004578.1 NA NA NA 0.2603987 NAPSPTO0621 NC_004578.1 NA NA NA 0.2456952 NAPSPTO0622 NC_004578.1 NA NA -0.103291 NA NAPSPTO0625 NC_004578.1 NA NA NA 0.2147073 NAPSPTO0626 NC_004578.1 NA NA NA NA NAPSPTO0628 NC_004578.1 NA NA NA 0.1819499 NAPSPTO0631 NC_004578.1 NA NA NA 0.1594127 NAPSPTO0632 NC_004578.1 NA NA NA 0.1565849 NAPSPTO0637 NC_004578.1 NA NA NA 0.1688892 NAPSPTO0638 NC_004578.1 NA NA NA 0.1649339 NAPSPTO0639 NC_004578.1 NA NA NA 0.1687956 NAPSPTO0642 NC_004578.1 NA NA NA 0.174371 NAPSPTO0644 NC_004578.1 NA NA NA NA NAPSPTO0647 NC_004578.1 NA NA NA 0.2158567 NAPSPTO0648 NC_004578.1 NA 0.3022635 NA 0.2412944 NAPSPTO0649 NC_004578.1 NA NA NA 0.208953 NAPSPTO0651 NC_004578.1 NA NA NA 0.234987 NAPSPTO0653 NC_004578.1 NA NA -3.539556 -3.450337 NA

Page 3: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO0655 NC_004578.1 NA 0.7125588 NA NA NAPSPTO0677 NC_004578.1 NA 0.8515075 NA 0.6929601 NAPSPTO0679 NC_004578.1 NA NA NA -2.302015 NAPSPTO0680 NC_004578.1 NA NA NA -1.910729 NAPSPTO0691 NC_004578.1 NA NA NA -0.422155 NAPSPTO0700 NC_004578.1 NA 0.6216295 NA NA NAPSPTO0703 NC_004578.1 NA NA NA -0.651079 NAPSPTO0727 NC_004578.1 NA NA NA -0.598146 NAPSPTO0728 NC_004578.1 NA -0.749113 NA -0.603822 NAPSPTO0763 NC_004578.1 NA NA NA 0.593547 NAPSPTO0776 NC_004578.1 NA NA NA -1.135762 NAPSPTO0777 NC_004578.1 NA NA NA -0.33865 NAPSPTO0778 NC_004578.1 NA NA NA -0.680834 NAPSPTO0796 NC_004578.1 NA 0.7042712 NA NA NAPSPTO0797 NC_004578.1 NA 0.4740566 NA NA NAPSPTO0799 NC_004578.1 NA NA NA NA NAPSPTO0805 NC_004578.1 NA 0.9193808 NA NA NAPSPTO0806 NC_004578.1 NA NA NA NA NAPSPTO0808 NC_004578.1 NA 0.660218 NA NA NAPSPTO0829 NC_004578.1 NA NA NA -0.467094 NAPSPTO0834 NC_004578.1 NA NA -1.093207 -0.858011 NAPSPTO0835 NC_004578.1 NA NA -0.837071 -0.827544 NAPSPTO0836 NC_004578.1 NA NA -1.783098 -1.505228 NAPSPTO0837 NC_004578.1 NA NA -1.232273 -1.066794 NAPSPTO0838 NC_004578.1 NA NA -1.249085 -1.297307 NAPSPTO0851 NC_004578.1 NA NA NA -1.783988 NAPSPTO0852 NC_004578.1 NA NA -1.244964 -2.186135 NAPSPTO5621 NC_004578.1 NA NA NA -1.50138 NAPSPTO0853 NC_004578.1 NA NA NA -0.813887 NAPSPTO0855 NC_004578.1 NA NA NA -1.191462 NAPSPTO0856 NC_004578.1 NA NA NA -1.24116 NAPSPTO0871 NC_004578.1 NA NA NA -0.9563 NAPSPTO0873 NC_004578.1 NA NA -0.537905 -0.685354 NAPSPTO0874 NC_004578.1 NA NA -1.005962 -1.270933 NAPSPTO0875 NC_004578.1 NA NA -2.219572 -2.925747 NAPSPTO0876 NC_004578.1 NA NA -0.643295 -1.101544 NAPSPTO0877 NC_004578.1 NA NA -0.989708 -1.954384 NAPSPTO0883 NC_004578.1 NA NA NA -1.916402 NAPSPTO0912 NC_004578.1 NA -2.000891 NA NA -2.016193PSPTO0927 NC_004578.1 NA -0.494575 NA NA NAPSPTO0929 NC_004578.1 NA NA NA NA NAPSPTO0940 NC_004578.1 NA NA NA -0.406008 NAPSPTO0944 NC_004578.1 NA NA NA -0.294466 NAPSPTO0945 NC_004578.1 NA -0.305507 NA -0.307427 NAPSPTO0946 NC_004578.1 NA NA NA NA NAPSPTO0954 NC_004578.1 NA NA NA -0.701972 NAPSPTO0955 NC_004578.1 NA NA NA -1.053288 NAPSPTO0959 NC_004578.1 NA NA NA -0.354038 NAPSPTO0960 NC_004578.1 NA NA NA NA NAPSPTO0961 NC_004578.1 NA NA NA NA NAPSPTO0975 NC_004578.1 NA NA NA NA NAPSPTO0976 NC_004578.1 NA NA NA -0.391145 NAPSPTO0978 NC_004578.1 NA NA NA -0.779764 NAPSPTO0989 NC_004578.1 NA 1.1254748 NA NA NAPSPTO0994 NC_004578.1 NA NA NA -0.5896 NAPSPTO1005 NC_004578.1 NA NA NA -0.312229 NAPSPTO1038 NC_004578.1 NA NA NA -0.625046 NAPSPTO1065 NC_004578.1 NA NA NA -0.655131 NA

Page 4: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO1069 NC_004578.1 NA 0.7434227 NA NA NAPSPTO1070 NC_004578.1 NA NA NA NA NAPSPTO1075 NC_004578.1 NA 1.5675323 NA NA NAPSPTO1080 NC_004578.1 NA 0.7090277 NA NA NAPSPTO1102 NC_004578.1 NA 1.0986236 NA 0.6827453 NAPSPTO1104 NC_004578.1 NA 0.5167661 NA NA NAPSPTO1134 NC_004578.1 NA NA NA 1.2205394 NAPSPTO1136 NC_004578.1 NA NA NA NA NAPSPTO1144 NC_004578.1 NA NA NA NA NAPSPTO1148 NC_004578.1 NA NA NA -0.667587 NAPSPTO1150 NC_004578.1 NA -0.891387 NA NA NAPSPTO1164 NC_004578.1 NA NA -0.593324 NA NAPSPTO1180 NC_004578.1 NA NA NA NA NAPSPTO1182 NC_004578.1 NA NA NA NA NAPSPTO1197 NC_004578.1 NA NA NA -0.426407 NAPSPTO1208 NC_004578.1 NA NA NA NA NAPSPTO1210 NC_004578.1 NA NA NA NA NAPSPTO1213 NC_004578.1 NA -0.691536 NA -0.615016 NAPSPTO1214 NC_004578.1 NA -2.95335 NA -2.559413 NAPSPTO1246 NC_004578.1 NA NA NA NA NAPSPTO1258 NC_004578.1 NA NA NA -0.706054 NAPSPTO1266 NC_004578.1 NA 0.3829357 NA 0.206712 NAPSPTO1275 NC_004578.1 NA NA NA 1.4569478 NAPSPTO1276 NC_004578.1 NA NA NA NA NAPSPTO1281 NC_004578.1 NA NA NA 0.7321407 NAPSPTO1283 NC_004578.1 NA NA NA NA NAPSPTO1284 NC_004578.1 NA NA NA NA NAPSPTO1287 NC_004578.1 NA -0.480772 NA -0.34375 NAPSPTO1288 NC_004578.1 NA NA NA -1.508038 NAPSPTO1289 NC_004578.1 NA NA NA -1.020779 NAPSPTO1290 NC_004578.1 NA NA NA -0.442841 NAPSPTO1292 NC_004578.1 NA NA NA NA NAPSPTO1295 NC_004578.1 NA NA NA -0.386217 NAPSPTO1296 NC_004578.1 NA NA NA -0.565699 NAPSPTO1299 NC_004578.1 NA NA NA -0.201315 NAPSPTO1300 NC_004578.1 NA NA NA -0.357844 NAPSPTO1301 NC_004578.1 NA NA NA -0.457383 NAPSPTO1302 NC_004578.1 NA NA NA -0.992063 NAPSPTO1304 NC_004578.1 NA NA -1.529705 NA NAPSPTO1340 NC_004578.1 NA NA NA -0.54878 NAPSPTO1369 NC_004578.1 NA NA -0.779718 -1.132222 NAPSPTO1370 NC_004578.1 NA NA -1.253259 -2.185717 NAPSPTO1371 NC_004578.1 NA NA NA -2.250218 NAPSPTO1372 NC_004578.1 NA NA -1.36767 -2.553906 NAPSPTO1373 NC_004578.1 NA NA NA -0.94733 NAPSPTO1374 NC_004578.1 NA NA -1.315215 -1.80583 NAPSPTO1375 NC_004578.1 NA NA -1.710335 -2.787776 NAPSPTO1377 NC_004578.1 NA NA NA -1.229378 NAPSPTO1378 NC_004578.1 NA NA -1.125562 -2.09983 NAPSPTO1379 NC_004578.1 NA NA -1.450967 -1.531823 NAPSPTO1380 NC_004578.1 NA NA -1.138472 -1.012976 NAPSPTO1381 NC_004578.1 NA NA NA -0.210347 NAPSPTO1382 NC_004578.1 NA NA NA -0.546063 NAPSPTO1383 NC_004578.1 NA NA -0.606977 -0.910963 NAPSPTO1384 NC_004578.1 NA NA -0.639693 -0.882134 NAPSPTO1385 NC_004578.1 NA NA -0.854927 -1.21181 NAPSPTO1386 NC_004578.1 NA NA -1.195371 -2.402792 NAPSPTO1387 NC_004578.1 NA 0.7416295 NA -0.878598 NA

Page 5: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO1388 NC_004578.1 NA NA NA -0.880623 NAPSPTO1389 NC_004578.1 NA NA -0.833506 -1.248336 NAPSPTO1390 NC_004578.1 NA NA -0.830914 -1.152631 NAPSPTO1391 NC_004578.1 NA NA -0.892835 -1.251592 NAPSPTO1394 NC_004578.1 NA NA NA -1.341711 NAPSPTO1395 NC_004578.1 NA NA -0.875173 -1.661899 NAPSPTO1396 NC_004578.1 NA NA -1.031415 -1.635579 NAPSPTO1397 NC_004578.1 NA NA NA -2.095955 NAPSPTO1398 NC_004578.1 NA NA -0.8623 -1.172721 NAPSPTO1399 NC_004578.1 NA NA -0.933078 -1.235075 NAPSPTO1400 NC_004578.1 NA NA -2.311183 -3.49863 NAPSPTO1401 NC_004578.1 NA NA -1.468183 -2.321517 NAPSPTO1402 NC_004578.1 NA NA -1.106257 -1.733231 NAPSPTO1403 NC_004578.1 NA NA NA -2.13161 NAPSPTO1404 NC_004578.1 NA NA -0.993666 -1.23282 NAPSPTO1405 NC_004578.1 NA NA -0.698289 -1.063583 NAPSPTO1406 NC_004578.1 NA NA -0.867342 -1.546165 NAPSPTO5622 NC_004578.1 NA NA NA -0.47389 NAPSPTO1408 NC_004578.1 NA NA -1.679169 -1.652313 NAPSPTO1409 NC_004578.1 NA NA -1.265226 -1.031571 NAPSPTO1414 NC_004578.1 NA 0.6190284 NA NA NAPSPTO1422 NC_004578.1 NA NA NA 0.6017408 NAPSPTO1423 NC_004578.1 NA NA NA NA NAPSPTO1429 NC_004578.1 NA 1.1379369 NA 0.6044363 NAPSPTO1431 NC_004578.1 NA 0.7103215 NA NA NAPSPTO1443 NC_004578.1 NA NA NA NA NAPSPTO1451 NC_004578.1 NA NA NA NA NAPSPTO1456 NC_004578.1 NA NA NA 0.4885487 NAPSPTO1468 NC_004578.1 NA NA NA NA NAPSPTO1472 NC_004578.1 NA NA NA NA NAPSPTO1473 NC_004578.1 NA 0.5127414 NA 0.3527128 NAPSPTO1474 NC_004578.1 NA 0.5896041 NA 0.4225533 NAPSPTO1475 NC_004578.1 NA 0.9941261 NA 0.684324 NAPSPTO1479 NC_004578.1 NA 0.7913766 NA NA NAPSPTO1506 NC_004578.1 NA NA -0.479555 NA NAPSPTO1507 NC_004578.1 NA NA -0.517034 NA NAPSPTO1508 NC_004578.1 NA NA NA -0.74502 NAPSPTO1509 NC_004578.1 NA NA NA NA NAPSPTO1529 NC_004578.1 NA 1.2176606 NA NA NAPSPTO1532 NC_004578.1 NA NA NA -0.559682 NAPSPTO1539 NC_004578.1 NA 1.0768934 NA NA NAPSPTO1541 NC_004578.1 NA NA NA -0.770984 NAPSPTO1543 NC_004578.1 NA 0.8440602 NA 0.4075718 NAPSPTO1544 NC_004578.1 NA 1.2407705 NA 0.6113917 NAPSPTO1545 NC_004578.1 NA 0.7912813 NA NA NAPSPTO1546 NC_004578.1 NA 0.8387536 NA NA NAPSPTO1547 NC_004578.1 NA 0.6797566 NA 0.4207038 NAPSPTO1548 NC_004578.1 NA 1.2675114 NA 0.523909 NAPSPTO1549 NC_004578.1 NA 0.883416 NA NA NAPSPTO1550 NC_004578.1 NA NA NA NA NAPSPTO1562 NC_004578.1 NA 0.7914621 NA NA NAPSPTO1563 NC_004578.1 NA NA NA 0.0889872 NAPSPTO1565 NC_004578.1 NA -1.181613 NA -0.751101 NAPSPTO1568 NC_004578.1 NA 1.495857 -2.54482 -2.88323 NAPSPTO5620 NC_004578.1 NA 2.2696233 NA NA NAPSPTO1593 NC_004578.1 NA 0.9519886 NA NA NAPSPTO1609 NC_004578.1 NA NA NA -0.968524 NAPSPTO1632 NC_004578.1 NA NA NA NA NA

Page 6: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO1633 NC_004578.1 NA NA -0.819942 0.9386739 NAPSPTO1646 NC_004578.1 NA NA NA -0.62994 NAPSPTO1648 NC_004578.1 NA -0.930496 NA NA NAPSPTO1684 NC_004578.1 NA NA -0.37973 NA NAPSPTO1687 NC_004578.1 NA 0.6520637 NA NA NAPSPTO1690 NC_004578.1 NA 0.3570938 NA NA NAPSPTO1695 NC_004578.1 NA NA NA 0.3372638 NAPSPTO1699 NC_004578.1 NA 0.5533897 NA NA NAPSPTO1708 NC_004578.1 NA NA NA -3.217811 NAPSPTO1719 NC_004578.1 NA NA NA -0.701776 NAPSPTO1720 NC_004578.1 NA NA 0.3976194 NA NAPSPTO1721 NC_004578.1 NA -0.867269 NA -0.618334 NAPSPTO1724 NC_004578.1 NA NA NA -1.297375 NAPSPTO1725 NC_004578.1 NA NA NA -0.651292 NAPSPTO1734 NC_004578.1 NA NA NA NA NAPSPTO1740 NC_004578.1 NA 0.8284356 NA NA NAPSPTO1745 NC_004578.1 NA NA NA NA NAPSPTO1749 NC_004578.1 NA NA NA 0.5692577 NAPSPTO1752 NC_004578.1 NA NA NA NA NAPSPTO1763 NC_004578.1 NA NA NA -0.29219 NAPSPTO1778 NC_004578.1 NA NA NA -1.100671 NAPSPTO1779 NC_004578.1 NA NA NA NA NAPSPTO1802 NC_004578.1 NA NA NA NA NAPSPTO1809 NC_004578.1 NA 0.5807564 NA NA NAPSPTO1817 NC_004578.1 NA NA NA -0.882354 NAPSPTO1839 NC_004578.1 NA NA NA NA NAPSPTO1843 NC_004578.1 NA 0.8001777 NA NA NAPSPTO1855 NC_004578.1 NA NA NA -2.353503 NAPSPTO1886 NC_004578.1 NA NA -1.47953 NA NAPSPTO1891 NC_004578.1 NA NA NA 1.3248494 NAPSPTO1902 NC_004578.1 NA NA NA 0.329977 NAPSPTO1916 NC_004578.1 NA NA NA NA NAPSPTO1930 NC_004578.1 NA NA NA NA NAPSPTO1934 NC_004578.1 NA NA 0.3854097 NA NAPSPTO1936 NC_004578.1 NA -0.661617 0.4620528 NA NAPSPTO1939 NC_004578.1 NA -0.673401 NA NA NAPSPTO1948 NC_004578.1 NA 0.5230275 NA NA NAPSPTO1949 NC_004578.1 NA -0.361506 NA NA NAPSPTO1950 NC_004578.1 NA NA NA NA NAPSPTO1951 NC_004578.1 NA -0.453567 NA NA NAPSPTO1977 NC_004578.1 NA NA NA NA NAPSPTO1979 NC_004578.1 NA NA NA 0.5047145 NAPSPTO2016 NC_004578.1 NA NA NA NA NAPSPTO2020 NC_004578.1 NA NA NA -0.325822 NAPSPTO2035 NC_004578.1 NA NA NA 0.4729637 NAPSPTO2047 NC_004578.1 NA NA NA -0.478379 NAPSPTO2049 NC_004578.1 -1.449981 NA NA NA NAPSPTO2052 NC_004578.1 NA 1.2004989 NA 0.2990735 NAPSPTO2057 NC_004578.1 NA NA NA -0.488341 NAPSPTO2099 NC_004578.1 NA NA NA 0.6865337 NAPSPTO2102 NC_004578.1 NA NA NA 0.3113617 NAPSPTO2104 NC_004578.1 NA 0.5037195 NA NA NAPSPTO2105 NC_004578.1 NA NA NA -1.267981 NAPSPTO2112 NC_004578.1 NA 0.3108759 NA NA NAPSPTO2124 NC_004578.1 NA NA NA -0.196824 NAPSPTO2128 NC_004578.1 NA NA NA -2.240612 NAPSPTO2130 NC_004578.1 NA NA NA -1.516483 NAPSPTO2133 NC_004578.1 NA NA NA NA NA

Page 7: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO2134 NC_004578.1 NA NA NA NA NAPSPTO2135 NC_004578.1 NA NA NA NA NAPSPTO2136 NC_004578.1 NA NA NA NA NAPSPTO2137 NC_004578.1 NA NA 4.8126395 5.0798361 NAPSPTO2138 NC_004578.1 NA NA NA NA NAPSPTO2139 NC_004578.1 NA NA NA NA NAPSPTO2141 NC_004578.1 NA NA NA NA NAPSPTO2142 NC_004578.1 NA NA NA 2.4137311 NAPSPTO2143 NC_004578.1 NA NA NA NA NAPSPTO2144 NC_004578.1 NA NA NA NA NAPSPTO2145 NC_004578.1 NA NA NA NA NAPSPTO2146 NC_004578.1 NA NA NA NA NAPSPTO2147 NC_004578.1 NA NA NA NA NAPSPTO2148 NC_004578.1 NA NA NA NA NAPSPTO2149 NC_004578.1 NA NA NA NA NAPSPTO2150 NC_004578.1 NA NA NA NA NAPSPTO2152 NC_004578.1 NA NA 7.3330339 7.3720057 NAPSPTO2153 NC_004578.1 NA NA NA NA NAPSPTO2154 NC_004578.1 NA NA NA NA NAPSPTO2155 NC_004578.1 NA NA NA NA NAPSPTO2156 NC_004578.1 NA NA NA NA NAPSPTO2160 NC_004578.1 NA NA NA NA NAPSPTO2161 NC_004578.1 NA NA NA NA NAPSPTO2172 NC_004578.1 NA NA NA -0.676743 NAPSPTO2173 NC_004578.1 NA NA NA NA NAPSPTO2174 NC_004578.1 NA NA NA NA NAPSPTO2175 NC_004578.1 NA NA NA -0.293379 NAPSPTO2176 NC_004578.1 NA NA NA -0.376981 NAPSPTO2179 NC_004578.1 NA NA NA -0.460676 NAPSPTO2186 NC_004578.1 NA NA NA NA NAPSPTO2193 NC_004578.1 NA -0.163047 NA NA NAPSPTO2195 NC_004578.1 NA 0.6762704 NA NA NAPSPTO2196 NC_004578.1 NA NA NA NA NAPSPTO2197 NC_004578.1 NA NA NA NA NAPSPTO2198 NC_004578.1 NA NA NA NA NAPSPTO2202 NC_004578.1 NA NA NA NA NAPSPTO2208 NC_004578.1 NA NA -0.228808 -0.154122 NAPSPTO2211 NC_004578.1 NA 0.4442514 NA NA NAPSPTO2254 NC_004578.1 NA NA NA -0.638025 NAPSPTO2274 NC_004578.1 NA NA NA NA NAPSPTO2275 NC_004578.1 NA 0.4097258 NA NA NAPSPTO2280 NC_004578.1 NA NA NA NA NAPSPTO2281 NC_004578.1 NA NA NA NA NAPSPTO2298 NC_004578.1 NA 0.2146595 NA 0.4531196 NAPSPTO2310 NC_004578.1 NA -1.653683 NA NA NAPSPTO2331 NC_004578.1 NA NA NA NA NAPSPTO2338 NC_004578.1 NA NA NA -2.376455 NAPSPTO2339 NC_004578.1 NA NA NA -1.222296 NAPSPTO2341 NC_004578.1 NA NA NA -0.291559 NAPSPTO2346 NC_004578.1 NA NA NA NA NAPSPTO2367 NC_004578.1 NA NA NA NA NAPSPTO2372 NC_004578.1 NA NA NA NA NAPSPTO2373 NC_004578.1 NA -0.460351 NA NA NAPSPTO2377 NC_004578.1 NA NA NA NA NAPSPTO2379 NC_004578.1 NA 0.3290287 NA 0.3586306 NAPSPTO2380 NC_004578.1 NA 0.2319766 NA 0.242557 NAPSPTO2381 NC_004578.1 NA 0.4007427 NA 0.3514488 NAPSPTO2382 NC_004578.1 NA NA NA 0.2765924 NA

Page 8: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO2479 NC_004578.1 NA -1.946275 NA NA NAPSPTO2506 NC_004578.1 NA NA NA 0.3724438 NAPSPTO2589 NC_004578.1 NA -2.507143 NA -2.080508 NAPSPTO2595 NC_004578.1 NA NA NA NA NAPSPTO2596 NC_004578.1 NA NA NA NA NAPSPTO2597 NC_004578.1 NA NA NA NA NAPSPTO2598 NC_004578.1 NA NA NA NA NAPSPTO2599 NC_004578.1 NA NA NA NA NAPSPTO2600 NC_004578.1 NA NA NA NA NAPSPTO2601 NC_004578.1 NA NA NA NA NAPSPTO2602 NC_004578.1 NA NA NA NA NAPSPTO2603 NC_004578.1 NA NA NA NA NAPSPTO2604 NC_004578.1 NA NA NA NA NAPSPTO2605 NC_004578.1 NA NA NA NA NAPSPTO2608 NC_004578.1 NA NA NA -1.480514 NAPSPTO2638 NC_004578.1 NA NA NA -1.333573 NAPSPTO2678 NC_004578.1 NA NA -1.014436 -1.923894 NAPSPTO2680 NC_004578.1 NA NA NA -0.93577 NAPSPTO2691 NC_004578.1 NA NA -0.970912 -1.769909 NAPSPTO2701 NC_004578.1 NA NA NA -0.541423 NAPSPTO2702 NC_004578.1 NA NA NA -0.445931 NAPSPTO2703 NC_004578.1 NA NA NA -0.342859 NAPSPTO2705 NC_004578.1 NA NA NA -0.397877 NAPSPTO2707 NC_004578.1 NA NA NA -0.38756 NAPSPTO2714 NC_004578.1 NA NA NA 0.3608413 NAPSPTO2719 NC_004578.1 NA NA NA -0.759138 NAPSPTO2720 NC_004578.1 NA NA NA -1.082981 NAPSPTO2729 NC_004578.1 NA NA NA NA NAPSPTO2730 NC_004578.1 NA NA NA NA NAPSPTO2732 NC_004578.1 NA 0.6976317 NA NA NAPSPTO2752 NC_004578.1 NA NA NA -0.398752 NAPSPTO2769 NC_004578.1 NA NA NA NA NAPSPTO2773 NC_004578.1 NA NA -0.673957 NA NAPSPTO2806 NC_004578.1 NA -0.936105 NA -0.777017 NAPSPTO2829 NC_004578.1 NA -1.097016 NA NA NAPSPTO2844 NC_004578.1 NA NA NA -2.754938 NAPSPTO2845 NC_004578.1 NA NA NA -1.874569 NAPSPTO2846 NC_004578.1 NA NA NA -0.808659 NAPSPTO2849 NC_004578.1 NA NA NA -1.852842 NAPSPTO2850 NC_004578.1 NA NA NA -2.289521 NAPSPTO2851 NC_004578.1 NA NA NA -2.263942 NAPSPTO2852 NC_004578.1 NA NA NA -2.500259 NAPSPTO2853 NC_004578.1 NA NA NA -3.529249 NAPSPTO2871 NC_004578.1 NA -0.687562 NA NA NAPSPTO2872 NC_004578.1 NA -0.729911 NA NA NAPSPTO2873 NC_004578.1 NA -0.448903 NA NA NAPSPTO2877 NC_004578.1 NA -0.90573 NA NA NAPSPTO2878 NC_004578.1 NA -0.696512 NA NA NAPSPTO2904 NC_004578.1 NA NA NA -1.327832 NAPSPTO3039 NC_004578.1 NA NA NA -0.537048 NAPSPTO3067 NC_004578.1 NA 1.7846943 NA NA NAPSPTO3087 NC_004578.1 NA NA -0.541941 -0.957291 NAPSPTO3105 NC_004578.1 NA NA NA -0.734545 NAPSPTO3108 NC_004578.1 NA -0.417724 NA NA NAPSPTO3117 NC_004578.1 NA 0.938612 NA NA NAPSPTO3120 NC_004578.1 NA NA 2.4163744 1.7678175 NAPSPTO3121 NC_004578.1 NA NA 1.0893436 1.4718353 NAPSPTO3122 NC_004578.1 NA NA 1.5228517 1.6000405 NA

Page 9: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO3130 NC_004578.1 NA NA NA NA NAPSPTO3136 NC_004578.1 NA NA NA -0.488499 NAPSPTO3150 NC_004578.1 NA NA NA -1.824131 NAPSPTO3152 NC_004578.1 NA NA NA -1.881223 NAPSPTO3157 NC_004578.1 NA NA NA 3.2856045 NAPSPTO3162 NC_004578.1 NA NA NA NA NAPSPTO3163 NC_004578.1 NA NA NA NA NAPSPTO3164 NC_004578.1 NA NA NA -0.72995 NAPSPTO3179 NC_004578.1 NA 0.4832257 NA NA NAPSPTO3195 NC_004578.1 NA NA NA -0.756483 NAPSPTO3269 NC_004578.1 NA NA NA -1.140144 NAPSPTO3278 NC_004578.1 NA NA NA -0.980588 NAPSPTO3282 NC_004578.1 NA NA NA -0.707853 NAPSPTO3291 NC_004578.1 NA NA NA -1.515826 NAPSPTO3294 NC_004578.1 NA NA 4.6611429 4.9833611 NAPSPTO3323 NC_004578.1 NA NA NA -0.711633 NAPSPTO3331 NC_004578.1 NA NA NA -0.373758 NAPSPTO3333 NC_004578.1 NA NA NA -0.890306 NAPSPTO3337 NC_004578.1 NA NA NA NA NAPSPTO3349 NC_004578.1 NA 0.450446 NA 0.5159807 NAPSPTO3352 NC_004578.1 NA 1.409974 NA NA NAPSPTO3353 NC_004578.1 NA NA NA -0.389868 NAPSPTO3355 NC_004578.1 NA -1.742254 NA -1.1227 NAPSPTO3359 NC_004578.1 NA 1.9989143 NA 0.6515201 NAPSPTO3364 NC_004578.1 NA NA NA NA NAPSPTO3365 NC_004578.1 NA NA NA NA NAPSPTO3366 NC_004578.1 NA NA NA NA NAPSPTO3367 NC_004578.1 NA NA NA NA NAPSPTO3368 NC_004578.1 NA NA NA -1.049964 NAPSPTO3369 NC_004578.1 NA NA NA NA NAPSPTO3370 NC_004578.1 NA NA NA -1.120013 NAPSPTO3371 NC_004578.1 NA NA NA NA NAPSPTO3373 NC_004578.1 NA NA NA NA NAPSPTO3376 NC_004578.1 NA NA NA NA NAPSPTO3377 NC_004578.1 NA NA NA -0.913131 NAPSPTO3380 NC_004578.1 NA NA NA -1.28414 NAPSPTO3381 NC_004578.1 NA NA NA -1.897646 NAPSPTO3382 NC_004578.1 NA NA NA -0.850319 NAPSPTO3383 NC_004578.1 NA NA NA -1.442726 NAPSPTO3430 NC_004578.1 NA 0.7165159 NA NA NAPSPTO3455 NC_004578.1 NA NA NA -1.009889 NAPSPTO3462 NC_004578.1 NA NA NA NA NAPSPTO3468 NC_004578.1 NA -0.319601 NA NA NAPSPTO3487 NC_004578.1 NA 1.8607512 NA NA NAPSPTO3493 NC_004578.1 NA NA NA -1.208602 NAPSPTO3494 NC_004578.1 NA NA NA -0.711643 NAPSPTO3495 NC_004578.1 NA NA NA -0.880025 NAPSPTO3498 NC_004578.1 NA NA NA -0.901221 NAPSPTO3510 NC_004578.1 NA NA NA -0.503395 NAPSPTO3514 NC_004578.1 NA 0.671213 NA NA NAPSPTO3517 NC_004578.1 NA NA NA 0.1836206 NAPSPTO3520 NC_004578.1 NA NA NA NA NAPSPTO3544 NC_004578.1 NA NA NA -0.992358 NAPSPTO3548 NC_004578.1 NA NA NA NA NAPSPTO3550 NC_004578.1 NA NA NA -0.716147 NAPSPTO3551 NC_004578.1 NA NA NA -0.48319 NAPSPTO3553 NC_004578.1 NA NA NA -0.815244 NAPSPTO3554 NC_004578.1 NA NA NA NA NA

Page 10: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO3574 NC_004578.1 NA NA 5.0776797 4.8034906 NAPSPTO3577 NC_004578.1 NA -1.592586 NA -1.102454 NAPSPTO3580 NC_004578.1 NA NA NA NA NAPSPTO3582 NC_004578.1 NA NA -3.225921 -2.726119 NAPSPTO3596 NC_004578.1 NA NA NA 0.92282 NAPSPTO3597 NC_004578.1 NA NA NA NA NAPSPTO3598 NC_004578.1 NA NA 4.7406768 4.8797721 NAPSPTO3599 NC_004578.1 NA NA 4.4080581 4.9908334 NAPSPTO3602 NC_004578.1 NA -3.699105 NA -0.81183 NAPSPTO3616 NC_004578.1 NA -2.048954 NA -1.464334 NAPSPTO3646 NC_004578.1 NA 0.717898 NA NA NAPSPTO3676 NC_004578.1 NA 1.0650308 NA NA NAPSPTO3688 NC_004578.1 NA NA NA NA NAPSPTO3690 NC_004578.1 NA -0.895134 NA NA NAPSPTO3692 NC_004578.1 NA NA NA NA NAPSPTO3700 NC_004578.1 NA NA -0.803881 NA NAPSPTO3705 NC_004578.1 NA -0.604621 NA NA NAPSPTO3706 NC_004578.1 NA -0.694214 NA NA NAPSPTO3711 NC_004578.1 NA 0.4015653 NA NA NAPSPTO3712 NC_004578.1 NA 0.7205934 NA NA NAPSPTO3713 NC_004578.1 NA NA NA -0.296937 NAPSPTO3715 NC_004578.1 NA 0.9022993 NA NA NAPSPTO3719 NC_004578.1 NA NA NA NA NAPSPTO3721 NC_004578.1 NA NA NA NA NAPSPTO3727 NC_004578.1 NA NA NA 0.1649594 NAPSPTO3733 NC_004578.1 NA 1.4586749 NA NA NAPSPTO3752 NC_004578.1 NA NA NA -0.582625 NAPSPTO3757 NC_004578.1 NA NA NA NA NAPSPTO3768 NC_004578.1 NA NA NA NA NAPSPTO3783 NC_004578.1 NA NA NA NA NAPSPTO3788 NC_004578.1 NA NA NA -0.300955 NAPSPTO3789 NC_004578.1 NA 0.7670066 NA NA NAPSPTO3815 NC_004578.1 NA NA NA NA NAPSPTO3825 NC_004578.1 NA NA NA -0.356748 NAPSPTO3830 NC_004578.1 NA 0.5284449 NA NA NAPSPTO3833 NC_004578.1 NA NA NA NA NAPSPTO3834 NC_004578.1 NA 1.2035041 NA NA NAPSPTO3836 NC_004578.1 NA 0.9193201 NA 0.6709119 NAPSPTO3864 NC_004578.1 NA NA NA -0.44846 NAPSPTO3872 NC_004578.1 NA 0.6124516 NA NA NAPSPTO3878 NC_004578.1 NA -2.567231 NA -1.23379 NAPSPTO3893 NC_004578.1 NA NA NA -0.3774 NAPSPTO3902 NC_004578.1 NA NA NA -0.380866 NAPSPTO3917 NC_004578.1 NA NA NA 0.2633399 NAPSPTO3925 NC_004578.1 NA -1.433025 NA -0.935669 NAPSPTO3950 NC_004578.1 NA NA NA 0.2802247 NAPSPTO3951 NC_004578.1 NA NA NA 1.0980829 NAPSPTO3954 NC_004578.1 NA 1.4228385 NA NA NAPSPTO3955 NC_004578.1 NA NA NA NA NAPSPTO3959 NC_004578.1 NA NA NA -0.729666 NAPSPTO3972 NC_004578.1 NA NA NA 0.266933 NAPSPTO3973 NC_004578.1 NA NA NA 0.8334443 NAPSPTO3974 NC_004578.1 NA 0.9635483 NA NA NAPSPTO3975 NC_004578.1 NA 0.7901969 NA NA NAPSPTO3976 NC_004578.1 NA 0.5740509 NA NA NAPSPTO3983 NC_004578.1 NA NA 0.6961416 NA NAPSPTO3984 NC_004578.1 NA NA NA -0.451192 NAPSPTO3987 NC_004578.1 NA NA NA -0.561897 NA

Page 11: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4001 NC_004578.1 NA NA NA -0.260368 NAPSPTO4010 NC_004578.1 NA 0.5616195 NA NA NAPSPTO4019 NC_004578.1 NA NA NA NA NAPSPTO4024 NC_004578.1 NA NA NA 0.8235047 NAPSPTO4027 NC_004578.1 NA 0.3339887 NA NA NAPSPTO4033 NC_004578.1 NA NA NA -0.597194 NAPSPTO4059 NC_004578.1 NA NA NA NA NAPSPTO4100 NC_004578.1 NA 0.251562 NA NA NAPSPTO4101 NC_004578.1 NA NA -0.731852 -1.258466 NAPSPTO4107 NC_004578.1 NA 0.8652321 NA NA NAPSPTO4108 NC_004578.1 NA NA NA -0.235334 NAPSPTO4136 NC_004578.1 NA NA 0.8332186 NA NAPSPTO4145 NC_004578.1 NA 0.6716128 0.4615454 0.863006 NAPSPTO4147 NC_004578.1 NA 0.5535101 NA 0.184051 NAPSPTO4155 NC_004578.1 NA NA NA NA NAPSPTO4157 NC_004578.1 NA 0.8492961 NA NA NAPSPTO4158 NC_004578.1 NA NA NA NA NAPSPTO4159 NC_004578.1 NA NA 6.426395 7.471834 NAPSPTO4160 NC_004578.1 NA NA -4.271013 -4.379085 NAPSPTO4168 NC_004578.1 NA NA NA -0.716317 NAPSPTO4169 NC_004578.1 NA NA NA NA NAPSPTO4171 NC_004578.1 NA NA NA -0.394095 NAPSPTO4172 NC_004578.1 NA NA NA -0.357847 NAPSPTO4173 NC_004578.1 NA NA NA -0.456383 NAPSPTO4174 NC_004578.1 NA NA NA -0.451412 NAPSPTO4196 NC_004578.1 NA NA NA NA NAPSPTO4210 NC_004578.1 NA 0.4483233 -0.487546 NA NAPSPTO4218 NC_004578.1 NA 1.2620061 NA NA NAPSPTO4219 NC_004578.1 NA 0.9847359 NA NA NAPSPTO4222 NC_004578.1 NA NA NA 0.366896 NAPSPTO4223 NC_004578.1 NA NA NA NA NAPSPTO4224 NC_004578.1 NA 0.5874914 NA 0.5829675 NAPSPTO4232 NC_004578.1 -4.230758 NA -4.283955 NA 4.238137PSPTO4233 NC_004578.1 NA NA -3.148023 NA NAPSPTO4234 NC_004578.1 -2.309098 NA -2.234802 NA NAPSPTO4250 NC_004578.1 NA NA NA NA NAPSPTO4284 NC_004578.1 NA NA NA -1.417173 NAPSPTO4285 NC_004578.1 NA NA NA -2.361196 NAPSPTO4290 NC_004578.1 NA NA NA -0.242169 NAPSPTO4296 NC_004578.1 NA 2.1419174 NA NA NAPSPTO4297 NC_004578.1 NA -1.412129 NA -1.894108 NAPSPTO4298 NC_004578.1 NA NA NA -1.038664 NAPSPTO4305 NC_004578.1 NA -0.347147 NA NA NAPSPTO4306 NC_004578.1 NA NA NA NA NAPSPTO4312 NC_004578.1 NA NA NA NA NAPSPTO4317 NC_004578.1 NA NA NA NA NAPSPTO4322 NC_004578.1 NA NA NA NA NAPSPTO4331 NC_004578.1 NA NA -0.389046 -0.575976 NAPSPTO4332 NC_004578.1 NA 1.278686 -1.10646 -0.978492 NAPSPTO4333 NC_004578.1 NA NA NA -1.630766 NAPSPTO4335 NC_004578.1 NA -1.027895 NA NA NAPSPTO4338 NC_004578.1 NA NA NA NA NAPSPTO4339 NC_004578.1 NA NA NA -0.893949 NAPSPTO4340 NC_004578.1 NA NA NA -0.384456 NAPSPTO4356 NC_004578.1 NA NA NA -0.286252 NAPSPTO4358 NC_004578.1 NA NA NA -0.496201 NAPSPTO4363 NC_004578.1 NA NA NA -1.449999 NAPSPTO4366 NC_004578.1 NA NA 5.6377242 2.2418911 NA

Page 12: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4367 NC_004578.1 NA NA 2.994826 2.2354584 NAPSPTO4368 NC_004578.1 NA NA 2.57355 0.985238 NAPSPTO4369 NC_004578.1 NA NA 1.6313637 0.8441955 NAPSPTO4373 NC_004578.1 NA NA NA -1.028701 NAPSPTO4374 NC_004578.1 NA NA NA -0.602566 NAPSPTO4379 NC_004578.1 NA NA -0.839514 NA NAPSPTO4380 NC_004578.1 NA NA 0.6457005 -0.524599 NAPSPTO4381 NC_004578.1 NA NA 1.8012265 2.1540737 NAPSPTO4400 NC_004578.1 NA 0.4663601 NA NA NAPSPTO4407 NC_004578.1 NA 0.55374 NA NA NAPSPTO4408 NC_004578.1 NA NA NA 0.3875176 NAPSPTO4410 NC_004578.1 NA NA NA 0.3584266 NAPSPTO4420 NC_004578.1 NA 1.5650329 NA NA NAPSPTO4423 NC_004578.1 NA 0.8461829 NA NA NAPSPTO4424 NC_004578.1 NA 0.8659288 NA NA NAPSPTO4426 NC_004578.1 NA NA NA 0.2131288 NAPSPTO4429 NC_004578.1 NA NA NA NA NAPSPTO4432 NC_004578.1 NA NA -0.464856 NA NAPSPTO4433 NC_004578.1 NA 0.6240521 NA 0.2110165 NAPSPTO4441 NC_004578.1 NA 0.6843958 NA NA NAPSPTO4442 NC_004578.1 NA 1.397263 NA 0.7856238 NAPSPTO4443 NC_004578.1 NA 0.4897405 NA NA NAPSPTO4444 NC_004578.1 NA 0.3032637 NA NA NAPSPTO4445 NC_004578.1 NA NA NA NA NAPSPTO4446 NC_004578.1 NA 1.2918167 NA NA NAPSPTO4450 NC_004578.1 NA 0.6796405 NA NA NAPSPTO4451 NC_004578.1 NA 0.3390795 NA NA NAPSPTO4452 NC_004578.1 NA 0.3322938 NA NA NAPSPTO4453 NC_004578.1 NA 0.7047676 NA NA NAPSPTO4456 NC_004578.1 NA 0.9695941 NA 0.8525176 NAPSPTO4459 NC_004578.1 NA NA NA NA NAPSPTO4460 NC_004578.1 NA NA NA NA NAPSPTO4461 NC_004578.1 NA NA NA NA NAPSPTO4473 NC_004578.1 NA 0.6535008 NA NA NAPSPTO4484 NC_004578.1 -0.555288 NA -0.599805 NA NAPSPTO4492 NC_004578.1 NA 0.6308662 NA NA NAPSPTO4493 NC_004578.1 NA 0.7680063 NA 0.6905054 NAPSPTO4494 NC_004578.1 NA 1.2938911 NA NA NAPSPTO4499 NC_004578.1 NA 1.3975678 NA 0.3371682 NAPSPTO4500 NC_004578.1 NA NA NA NA NAPSPTO4503 NC_004578.1 NA 1.3940212 NA NA NAPSPTO4504 NC_004578.1 NA 1.3170737 NA NA NAPSPTO4505 NC_004578.1 NA 0.31986 NA NA NAPSPTO4506 NC_004578.1 NA 0.3513041 NA NA NAPSPTO4507 NC_004578.1 NA -0.583783 NA -0.897708 NAPSPTO4509 NC_004578.1 NA 0.7488658 NA NA NAPSPTO4515 NC_004578.1 NA 0.9561861 NA NA NAPSPTO4516 NC_004578.1 NA NA NA 1.1721081 NAPSPTO4530 NC_004578.1 NA NA NA -0.707174 NAPSPTO4543 NC_004578.1 NA NA NA -0.219457 NAPSPTO4547 NC_004578.1 NA NA NA NA NAPSPTO4557 NC_004578.1 NA NA NA -0.576592 NAPSPTO4558 NC_004578.1 NA NA 0.7495851 -0.79195 NAPSPTO4560 NC_004578.1 NA NA 1.5097239 -1.235339 NAPSPTO4561 NC_004578.1 NA NA NA NA NAPSPTO4562 NC_004578.1 NA NA NA -1.450949 NAPSPTO4573 NC_004578.1 NA 0.5384356 NA NA NAPSPTO4575 NC_004578.1 NA NA NA NA NA

Page 13: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4577 NC_004578.1 NA 1.0700018 NA 1.0163667 NAPSPTO4578 NC_004578.1 NA 1.585444 NA 1.6063946 NAPSPTO4579 NC_004578.1 NA 1.336162 NA NA NAPSPTO4580 NC_004578.1 NA NA NA NA NAPSPTO4582 NC_004578.1 NA NA NA -0.546836 NAPSPTO4583 NC_004578.1 NA NA NA NA NAPSPTO4585 NC_004578.1 NA NA NA NA NAPSPTO4588 NC_004578.1 NA NA -1.254524 -2.085412 NAPSPTO4589 NC_004578.1 NA NA -0.958698 -1.580561 NAPSPTO4597 NC_004578.1 NA 1.4172981 -1.274476 -1.8858 NAPSPTO4599 NC_004578.1 NA NA -0.854476 -1.418736 NAPSPTO4605 NC_004578.1 NA NA NA NA NAPSPTO4610 NC_004578.1 NA NA NA 1.5505564 NAPSPTO4611 NC_004578.1 NA NA NA 1.593792 NAPSPTO4612 NC_004578.1 NA NA NA NA NAPSPTO4613 NC_004578.1 NA NA NA 1.585852 NAPSPTO4638 NC_004578.1 NA NA NA -0.810619 NAPSPTO4646 NC_004578.1 NA NA NA -1.740455 NAPSPTO4647 NC_004578.1 NA NA NA -3.151012 NAPSPTO4648 NC_004578.1 NA NA NA -2.499857 NAPSPTO4667 NC_004578.1 NA NA NA NA NAPSPTO4681 NC_004578.1 NA NA NA -0.164576 NAPSPTO4682 NC_004578.1 NA NA NA -0.231434 NAPSPTO4683 NC_004578.1 NA NA NA NA NAPSPTO4685 NC_004578.1 NA NA NA -0.257303 NAPSPTO4686 NC_004578.1 NA NA NA -0.328762 NAPSPTO4687 NC_004578.1 NA NA NA -0.411068 NAPSPTO4689 NC_004578.1 NA NA NA -0.287093 NAPSPTO4690 NC_004578.1 NA NA NA -0.329838 NAPSPTO4691 NC_004578.1 NA NA -1.666178 -2.28565 NAPSPTO4703 NC_004578.1 NA NA -1.067705 -1.018289 NAPSPTO4704 NC_004578.1 NA NA -1.306811 -1.312865 NAPSPTO4712 NC_004578.1 NA 1.0470321 NA NA NAPSPTO4713 NC_004578.1 NA 1.2485108 NA NA NAPSPTO4714 NC_004578.1 NA NA NA NA NAPSPTO4718 NC_004578.1 NA NA -0.984917 -1.992003 NAPSPTO4720 NC_004578.1 NA NA NA -0.507764 NAPSPTO4721 NC_004578.1 NA NA NA -0.530916 NAPSPTO4723 NC_004578.1 NA 0.9503013 NA NA NAPSPTO4727 NC_004578.1 NA NA -1.465706 -3.526454 NAPSPTO4733 NC_004578.1 NA NA NA -1.930883 NAPSPTO4752 NC_004578.1 NA NA NA -0.56406 NAPSPTO4762 NC_004578.1 NA NA NA NA NAPSPTO4766 NC_004578.1 NA NA NA -1.070108 NAPSPTO4776 NC_004578.1 NA NA -0.704359 -0.852561 NAPSPTO4782 NC_004578.1 NA NA NA -1.061905 NAPSPTO4805 NC_004578.1 NA 0.4428268 NA NA NAPSPTO4807 NC_004578.1 NA 0.5835702 NA 0.4328318 NAPSPTO4818 NC_004578.1 NA NA NA NA NAPSPTO4822 NC_004578.1 NA NA NA NA NAPSPTO4849 NC_004578.1 NA NA NA NA NAPSPTO4862 NC_004578.1 NA 0.5323864 NA NA NAPSPTO4892 NC_004578.1 NA NA NA -0.651765 NAPSPTO4897 NC_004578.1 NA NA -0.449264 NA NAPSPTO4903 NC_004578.1 NA NA NA NA NAPSPTO4919 NC_004578.1 NA NA NA -1.074224 NAPSPTO4921 NC_004578.1 NA 0.5372033 NA NA NAPSPTO4923 NC_004578.1 NA NA NA NA NA

Page 14: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4933 NC_004578.1 NA NA NA 0.2722594 NAPSPTO4941 NC_004578.1 NA 0.4511618 NA NA NAPSPTO4943 NC_004578.1 NA NA NA 0.7293258 NAPSPTO4955 NC_004578.1 NA NA NA -0.637728 NAPSPTO4956 NC_004578.1 NA NA NA NA NAPSPTO4963 NC_004578.1 NA NA NA NA NAPSPTO4983 NC_004578.1 NA 0.2872357 NA NA NAPSPTO4992 NC_004578.1 NA NA NA NA NAPSPTO5034 NC_004578.1 NA NA NA 0.3225727 NAPSPTO5046 NC_004578.1 NA 0.5763849 NA NA NAPSPTO5048 NC_004578.1 NA NA NA NA NAPSPTO5049 NC_004578.1 NA NA NA 0.2373549 NAPSPTO5071 NC_004578.1 NA NA NA NA NAPSPTO5072 NC_004578.1 NA NA NA NA NAPSPTO5087 NC_004578.1 NA -1.321346 NA NA -1.240727PSPTO5090 NC_004578.1 NA NA NA NA NAPSPTO5123 NC_004578.1 NA NA NA -0.916493 NAPSPTO5140 NC_004578.1 NA NA NA -0.351924 NAPSPTO5141 NC_004578.1 NA 0.5035041 NA NA NAPSPTO5142 NC_004578.1 NA 1.2662469 NA NA NAPSPTO5147 NC_004578.1 NA -0.899395 NA -0.509582 NAPSPTO5154 NC_004578.1 NA 0.3567984 NA 0.3378382 NAPSPTO5175 NC_004578.1 NA -1.062133 NA -0.547935 NAPSPTO5177 NC_004578.1 NA NA NA NA NAPSPTO5240 NC_004578.1 NA 0.6060353 NA NA NAPSPTO5255 NC_004578.1 NA NA NA -0.761021 NAPSPTO5256 NC_004578.1 NA NA NA -1.578395 NAPSPTO5261 NC_004578.1 NA NA NA 0.805761 NAPSPTO5292 NC_004578.1 NA NA NA -0.576402 NAPSPTO5293 NC_004578.1 NA NA NA -0.751809 NAPSPTO5294 NC_004578.1 NA NA NA 0.31427 NAPSPTO5309 NC_004578.1 NA NA 0.6769667 NA NAPSPTO5310 NC_004578.1 NA NA 0.3602312 NA NAPSPTO5318 NC_004578.1 NA -0.882317 NA NA NAPSPTO5325 NC_004578.1 NA 0.9899235 NA NA NAPSPTO5326 NC_004578.1 NA 0.8926371 NA NA NAPSPTO5328 NC_004578.1 NA 0.6220496 NA 0.5237666 NAPSPTO5329 NC_004578.1 NA NA NA 0.3573404 NAPSPTO5336 NC_004578.1 NA 1.5177671 NA 0.6021311 NAPSPTO5337 NC_004578.1 NA 1.3834969 NA NA NAPSPTO5351 NC_004578.1 NA NA -0.92306 0.7961784 NAPSPTO5353 NC_004578.1 NA 1.3708249 -1.052439 -1.208247 NAPSPTO5354 NC_004578.1 NA NA -0.736302 -1.151489 NAPSPTO5355 NC_004578.1 NA NA NA -0.677055 NAPSPTO5377 NC_004578.1 NA 2.5588455 NA 2.8623793 NAPSPTO5378 NC_004578.1 NA 3.8950923 NA 3.2728285 3.888454PSPTO5379 NC_004578.1 NA 2.5138799 NA 1.6877618 2.483949PSPTO5380 NC_004578.1 NA 3.2082837 NA 2.8727085 3.282701PSPTO5381 NC_004578.1 NA 3.7296646 NA 3.0217049 3.310662PSPTO5385 NC_004578.1 NA -1.983809 NA NA NAPSPTO5392 NC_004578.1 NA NA NA NA NAPSPTO5397 NC_004578.1 NA NA NA NA NAPSPTO5402 NC_004578.1 NA NA NA NA NAPSPTO5407 NC_004578.1 NA -2.026948 NA -1.42497 NAPSPTO5422 NC_004578.1 NA -0.839477 NA NA NAPSPTO5432 NC_004578.1 NA NA NA NA NAPSPTO5433 NC_004578.1 NA -0.504055 NA NA NAPSPTO5435 NC_004578.1 NA -0.503068 NA NA NA

Page 15: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO5452 NC_004578.1 NA NA NA -0.434736 NAPSPTO5453 NC_004578.1 NA NA NA NA NAPSPTO5466 NC_004578.1 NA NA NA -0.73141 NAPSPTO5472 NC_004578.1 NA NA NA -0.623736 NAPSPTO5473 NC_004578.1 NA NA NA NA NAPSPTO5474 NC_004578.1 NA 0.8582477 NA NA NAPSPTO5499 NC_004578.1 NA NA NA 0.4213667 NAPSPTO5500 NC_004578.1 NA NA NA 0.5594313 NAPSPTO5505 NC_004578.1 NA NA -0.760622 NA NAPSPTO5506 NC_004578.1 NA NA NA NA NAPSPTO5507 NC_004578.1 NA NA -0.983131 NA NAPSPTO5510 NC_004578.1 NA NA NA -0.831729 NAPSPTO5511 NC_004578.1 NA NA NA -0.58515 NAPSPTO5517 NC_004578.1 NA NA NA -0.759383 NAPSPTO5520 NC_004578.1 NA NA NA NA NAPSPTO5522 NC_004578.1 NA NA NA -0.501934 NAPSPTO5537 NC_004578.1 NA -0.537556 NA NA NAPSPTO5599 NC_004578.1 NA NA NA 0.1730701 NAPSPTO5607 NC_004578.1 NA NA NA 0.3362539 NAPSPTO5608 NC_004578.1 NA NA NA 0.2914264 NAPSPTO5613 NC_004578.1 NA 1.3730886 NA 0.4806025 NAPSPTO5614 NC_004578.1 NA 0.7067067 NA 0.5010452 NAPSPTO_B0005 NC_004632.1 NA NA -0.598869 -0.896596 NAPSPTO_B0007 NC_004632.1 NA NA NA NA NAPSPTO_B0010 NC_004632.1 NA NA NA -0.393069 NAPSPTO_B0012 NC_004632.1 NA 0.5522179 NA -0.605545 NAPSPTO_B0025 NC_004632.1 NA NA NA -0.648474 NAPSPTO_B0026 NC_004632.1 NA NA NA -0.777345 NAPSPTO_B0027 NC_004632.1 NA NA NA -0.68997 NAPSPTO_B0071 NC_004632.1 NA -0.638941 NA -0.503609 NAPSPTOA0007 NC_004633.1 NA NA NA -0.511519 NAPSPTOA0008 NC_004633.1 NA -1.045962 NA -0.660665 NAPSPTOA0009 NC_004633.1 NA -0.982781 NA -0.631442 NAPSPTOA0011 NC_004633.1 NA NA NA -1.183121 NAPSPTOA0012 NC_004633.1 NA NA -0.744616 -1.373186 NAPSPTOA0017 NC_004633.1 NA NA -0.666939 -0.898187 NAPSPTOA0018 NC_004633.1 NA NA NA -0.885862 NAPSPTOA0019 NC_004633.1 NA NA -0.8416 -1.21726 NAPSPTOA0031 NC_004633.1 NA NA NA NA NAPSPTOA0036 NC_004633.1 NA 1.2479417 NA NA NAsmall RNA RsmY NC_004578.1 NA -0.453268 NA NA NA

NC_004578.1 NA NA 7.7506725 6.7324644 NAsmall RNA cobalamin-4 NC_004578.1 NA NA 2.7252975 1.6521049 NAsmall RNA P1 NC_004578.1 NA 0.6028795 NA 0.6604825 NA

small RNA prrF2

Page 16: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

b-/b+ c-/c+ b+/c+ nameNA NA NA recFNA NA NANA -1.004081 -0.836587NA NA NANA -2.569791 NA hopK1NA -1.837164 NA hopY1NA NA 4.6206006NA NA NANA 5.2431938 NA tonB-1NA 6.4724107 NA exbD-17.4606887 8.8815456 NA exbB-1NA NA NANA -0.214474 NA spoTNA -1.319921 NA gmkNA NA -0.678637NA NA -0.695634NA NA NA dadANA NA NANA NA NA repNA -1.529616 NA argHNA NA -0.63841 algQNA NA -0.225954NA NA NA prlCNA NA 1.1990988 osmCNA NA 0.8234983NA NA 1.1969337NA -0.875973 NANA NA -0.554266NA NA NANA NA -0.857731NA NA NANA NA NANA NA NA iucDNA NA -0.478003 glnKNA NA 1.3124878NA NA 0.8783491NA NA -0.969471NA NA NA pckANA NA NANA NA 2.3986034NA NA 2.7213842NA NA NA sbpNA NA 1.3632425 cysT

4.117592 3.2081509 NANA -0.235356 NA gcvT-1NA -0.545031 NANA NA NA gshANA NA -0.676925 ompRNA NA 2.7292792NA NA -1.307261NA NA NA glnA-1NA NA 0.3051484 typANA -1.179315 -0.40516 iaaLNA 1.152608 NA metKNA NA NA epdNA NA NA

: Differentially regulated genes identified at a p value less than or equal to 0.05 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 17: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NANA NA NA1.0960175 NA NANA NA NA rpoHNA NA 0.509312 thiSNA NA NA thiGNA NA NA badHNA NA -0.981522NA NA -0.813928 fdhA-1NA NA -1.232993NA -2.096007 -0.711723 shcFNA NA NA pqqE-2.434251 -2.725466 NA

NA NA NA rpsUNA NA -2.604232NA NA -1.512547NA NA -1.114781NA NA NA apaHNA NA NA apaGNA NA NA ksgANA NA NA pdxANA -0.56559 NA gphNA NA -0.212725 trpENA NA -1.563118NA NA -1.576779NA NA -0.768259-0.865567 -1.522258 -0.432264 hopH1-0.948114 -1.330995 NA hopC1

NA NA -0.591814 trpCNA -1.478206 NA speDNA -0.824158 NANA -1.333644 NANA NA -0.311549 argCNA NA -0.571932NA NA NA tyrSNA NA NA secENA NA NA nusGNA NA NA rplKNA NA NA rplANA NA NA rplJNA NA 0.2794107 rplLNA NA 0.3482859 rpsLNA NA NA rpsGNA NA 0.2695531 rpsJNA NA 0.1643509 rplCNA NA NA rplWNA NA NA rplVNA NA 0.1882195 rpsCNA NA 0.2358239 rplXNA NA 0.198757 rplENA NA NA rpsNNA NA NA rplRNA NA 0.1961934 rpmDNA NA 0.1917398 rpmJNA NA 0.2722516 rpsMNA NA 0.1712842 rpsKNA NA 0.272706 rpoANA -4.392562 NA

Page 18: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NANA NA NANA NA NANA NA NANA -0.514155 -0.396333 ribENA NA NA xseBNA NA -1.191336NA NA NA eutBNA NA -0.710799NA 0.8415704 NA fecBNA NA -1.192894 recCNA NA NA recBNA NA -0.672602 recDNA -0.759389 NA ispBNA NA NA rplUNA -0.410093 NANA -0.912874 NA ribFNA -0.98789 NA ileSNA -0.53482 NANA -0.869921 NA clpBNA -2.371836 NANA -1.554697 NANA -4.55163 NANA -2.715264 NANA -4.386666 NANA -2.631302 -1.288898NA -1.869806 -0.941171 hopAJ1NA NA NANA -0.498454 -0.733131NA -1.188587 NANA NA NANA -1.408731 NANA NA NANA -1.656948 NANA -3.60018 NA-0.854128 -1.136097 -0.458249 hopD1-1.164692 -1.889711 -0.964677 hopQ1-1

NA -1.250294 -1.036829 hopR1NA 1.9722201 NANA NA -0.46868NA NA -0.64831 gsTNA NA -0.295267 terZNA NA -0.364826 terDNA NA NA terENA NA -0.742699NA -0.587486 -0.712299NA -0.949544 -1.075107 fruKNA NA -0.312322 pgiNA -0.842526 NA panCNA -0.60022 NA panBNA NA -0.474312NA NA NANA NA NANA NA 0.6925469NA -0.716451 -0.477401NA NA -0.419114 gmdNA NA NANA NA -0.758844

Page 19: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NANA -0.545294 NANA NA NANA NA NA rfbDNA NA NA pthNA -0.400513 NA prsANA NA 1.3432154NA NA -0.473191 mqoNA NA -0.368152NA NA -1.051331 alkKNA NA -0.983086NA NA 0.9975487NA -0.455021 NANA NA -0.757079 folENA NA -0.442777NA 2.7620638 NANA 1.2632857 NANA NA -0.741642NA NA -3.114861NA NA -0.552907NA NA NANA NA NANA NA 2.1911293 gcvT-2NA NA 1.6334227 gcvPNA NA NANA 4.8351839 NANA 4.8284418 NANA NA -0.499937 gap-1NA NA -0.751593 eddNA -0.771565 NA glkNA NA -0.333095NA NA -0.778548NA NA NA gltKNA NA -0.576268 oprBNA NA NA hexRNA NA -0.588118 zwf-1NA NA -0.584589 pglNA NA -1.215476 eda-1NA NA 1.4541544NA NA -0.925166NA -1.316473 -0.352505NA -2.227402 -0.932458 hopN1NA -1.323891 -1.503786NA -2.561653 -1.186236 hopAA1-1NA -0.58987 -0.607316 hrpW1-1.535871 -2.115172 -0.490616 shcM

NA -2.822233 NA hopM1NA -1.173796 NA avrE1NA -2.406927 -0.974268NA -2.414211 NA hrpRNA -1.340359 NA hrpSNA NA NA hrpA1NA NA NA hrpZ1NA -1.34125 NA hrpB(Pto)NA -1.311128 NA hrcJNA -1.611665 NA hrpDNA -2.790877 -1.207421 hrpENA -1.620227 NA hrpF

Page 20: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA -1.393513 NA hrpGNA -1.425796 NA hrcC-0.888026 -1.321 NA hrpT-1.119342 -1.779791 NA hrpV

NA NA NA hrcS-0.979669 -1.751173 NA hrcR-1.419277 -1.888264 -0.604164 hrcQb

NA -2.364174 NA hrcQaNA -1.652615 -0.310421 hrpPNA -1.735737 NA hrpONA -4.469206 -1.187447 hrcNNA -2.537096 -0.853334 hrpQ-1.391817 -2.053826 -0.626974 hrcV

NA -2.508559 -1.311557 hrpJ-1.257698 -1.729669 NA hrpL

-0.89739 -0.964165 -0.365294 hrpK1NA -1.521306 NA hopB1NA NA NANA -2.976955 NANA -2.312567 NANA NA NA yajCNA NA NANA -0.46402 NA iscSNA NA NANA -0.753825 NANA NA -0.318851 bcpANA NA -0.265382NA 0.4886698 NA cumANA -1.049748 NA purTNA -0.681385 NA ffhNA NA NA rpsPNA NA NA rimMNA NA 0.6063817 trmDNA -0.730883 NA dsbCNA NA 0.687204NA NA 0.9302884NA NA -0.858277 ppcNA -0.531011 NA adkNA -0.736514 NANA NA NA glnDNA NA NA cdsA-1NA -0.586121 NANA NA NANA NA NA lpxDNA -0.546039 NA fabZNA NA NA lpxANA NA 0.5082461 lpxBNA NA NA rnhBNA NA NA dnaENA -0.451401 NA accANA -0.548192 NA surENA NA NA pcmNA NA -1.153686 rpoS-2.819862 -4.379087 NA hopAF1

NA -2.949454 NANA -0.639368 NANA -0.761407 -0.682927NA NA 1.8030315

Page 21: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA 1.7586162 asnBNA NA NANA 0.9310545 NA aer-1NA NA NANA -0.569879 NA arsCNA NA NANA NA NANA NA NA purNNA -3.033858 NA cobONA NA -0.923111NA NA -0.485225NA NA -0.696213NA NA -1.253753NA NA -0.932009NA -0.611617 NANA NA NANA NA 0.4055484 gyrANA NA 0.4510183 cmkNA NA -1.706016NA NA NANA NA NA htpXNA -0.272554 NANA 3.0312044 NANA NA NA ispZNA NA -0.689563NA NA -0.681104 ribHNA -0.751195 NANA NA NANA NA 1.5761409 sdaANA NA 2.5796829 pcDNA NA NA bphPNA 0.7034288 NANA NA -0.996594 cynSNA NA -0.436527 flgCNA NA -0.57689 flgE-1NA NA NA flgFNA NA NANA 0.3802949 NANA 0.4164798 NANA NA NA fliDNA NA -0.743558 flhFNA NA NA fliANA NA 0.3680535 acnANA NA NANA NA NA folENA -1.005384 NANA NA 2.0469486NA -0.901425 NANA NA NANA NA NANA NA NA gap-2NA NA NANA -1.705116 NANA NA NANA NA NANA -2.247789 -1.752758NA -1.571067 NANA 8.6313434 NA

Page 22: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA 7.2229953 NANA 7.4033246 NA pvsANA 7.7178646 NA daTNA 9.0235798 NANA 1.2403556 NANA 1.2342227 NANA 3.9797651 NANA 4.4037076 NANA 4.3252334 NANA 4.4420539 NANA 6.4421761 NANA 8.3829504 NANA 6.9997605 NANA 7.5205386 NANA 7.9845291 NANA 7.081217 NANA 11.478055 NANA 7.2532631 NA pvdENA 8.953826 NANA 3.4822469 NANA 8.3864441 NANA 3.9909763 NANA 7.919867 NANA -0.712966 -0.818386NA -1.425854 NA leuCNA -1.405381 NA leuDNA -0.32972 NA leuBNA -0.37283 NA asd-1NA NA -0.795786NA NA -0.447988 etfA-2NA NA NANA -0.79397 0.2654248 sdhCNA -0.863482 0.2683608NA -0.802474 NA sdhANA -0.447865 NA sdhBNA 0.5367724 NA sucCNA -0.288329 NA htpGNA -0.257054 NA fabANA NA NANA NA -1.035173NA -0.731734 NA aroF-1NA -1.783935 NA cysHNA -0.807766 -0.780658NA NA 0.4828151NA NA -1.429728 rmfNA NA -0.830807NA -3.314767 NA pcaHNA -1.724496 NA pcaGNA NA NA pcaBNA NA -0.669105NA NA -0.471187 rbsB-1NA -0.580862 -0.501622NA NA -0.320655NA NA 1.0263846NA NA 0.2979876 infCNA NA 0.2264506 rpmINA NA 0.3272639 rplTNA NA NA pheS

Page 23: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NANA NA 0.6241512NA NA -2.097998NA 7.3551667 NA pchANA 8.1597244 NA pchBNA 8.2557732 NA irp5NA 9.2882023 NA irp4NA 8.6616767 NA irp3NA 10.3148 NA irp1NA 9.8562613 NANA 10.275206 NANA 8.8035334 NANA 7.144291 NANA 9.3737924 NANA -2.168869 NANA NA -1.687486 abP-1.361635 -1.863967 -0.909458 hopP1

NA NA NA gabD-3-0.99366 -1.815677 NA

NA NA -0.58618NA NA NA xylBNA NA NA uxuBNA NA -0.555793NA NA -0.554632NA NA NANA -1.032754 -0.619126NA NA -1.004752 nudCNA NA 1.8881571NA NA 1.2288643 cysINA NA NA metHNA NA -0.551873 tpxNA NA 1.5273572NA NA 1.008277NA NA -0.770695NA NA NANA NA -2.253276NA NA -1.658941NA NA -0.828524NA -1.874796 NANA NA -1.701148NA NA -1.44088NA NA -2.648973NA NA -2.794836NA NA NANA NA NA hopL1NA NA NANA NA NANA NA NANA -1.383172 NA vanANA -0.575775 -0.679429NA NA 1.8270931NA -1.072279 -0.41535 hopAB2NA NA -0.686059NA NA NA ahpCNA -0.71491 NA2.4196308 2.1399956 NANA 1.9114979 NA zwf-2

1.846405 2.0177668 NA gnd

Page 24: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA 1.0711933 glgXNA NA NA acpDNA NA NANA NA NANA 7.3413133 NANA -1.017873 NANA NA -0.566295NA NA -0.768575 phbA-2NA NA NANA NA NANA NA -1.141973 pstSNA -0.946256 -1.133383NA NA -0.903342NA NA -1.892764NA 6.0026651 NANA NA -1.077138NA -0.368672 NANA NA -0.835678NA -1.19748 -1.132503NA NA 0.7935456 ftsKNA -0.911861 NA infANA NA -0.55455 clpANA NA NANA NA NANA -0.701358 -0.712302 aceANA -1.290635 NA nuoANA -0.809725 NA nuoBNA -1.290678 NA nuoCDNA -1.82099 NA nuoENA -1.774913 NA nuoFNA -1.969694 NA nuoGNA -2.873966 NA nuoHNA -4.269571 NA nuoJNA -1.890492 NA nuoMNA -1.742422 NA nuoNNA -1.707997 -1.090055NA -2.138914 -1.549655NA -1.220539 NANA -1.653615 NANA NA NANA NA -1.082239NA 5.4455626 NANA NA NANA NA 0.7760895NA NA -1.424707NA NA NA iolGNA NA -1.038047NA NA -1.012527NA -0.946908 NA lexA-2NA -0.541629 NA topANA NA NA fadBNA NA -0.49797NA NA -1.045906NA NA -1.433703NA NA -0.856498 fahANA NA -0.717647 hmgANA -1.099268 -1.104574 hppDNA -0.95956 NA maiA

Page 25: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA 6.0741522 NANA NA NANA NA 1.2333936-3.194291 -3.149391 NA katB

NA 1.1935497 NANA 0.9521692 NANA 5.9791688 NA4.3661633 6.006367 NANA NA NANA NA -1.308926NA NA NA dnaZXNA NA NANA 0.0375975 NANA 1.2500272 NANA 3.080949 NANA NA 0.5954741NA NA -0.861465NA NA NA acdANA NA NA dnaQNA NA NA rnhANA NA NANA NA NA mltDNA NA -0.180744NA -0.699694 NA fabINA NA NA tigNA -1.309743 NA folD-2NA -0.671877 NA acnBNA NA -0.537025NA -0.670426 NANA NA -0.74365NA -0.318018 NA pepNNA NA NANA -0.377489 NA accDNA -0.434702 NA pilZNA -0.808017 NA fabFNA -0.460319 NA fabDNA NA NA plsXNA NA 0.6143344NA NA NA psyINA NA NA minCNA NA NANA NA -0.401272NA NA -0.572722 cysKNA NA 0.5408889NA NA -1.45071NA NA NA purCNA NA NANA NA NANA NA -0.434835NA -1.263039 NA nadANA NA NA tolBNA NA 1.2030271 tolANA -0.887781 NA tolR-2NA NA NA tolQ-2NA NA NANA NA -0.518889NA NA NANA NA -0.503488 oprD

Page 26: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NA avrPto1NA NA NANA -2.378661 NANA NA 0.9497262 fnr-1NA -0.325878 NANA NA -0.627148 recANA -1.204043 NA fdxANA NA NANA -1.202933 -0.526614 hopAK1NA NA NANA NA -0.546846NA NA -1.303302NA NA 0.4014606 capBNA NA NA metGNA NA 0.3701799 argGNA NA NANA NA 0.2729259 rnt6.4141346 8.6726328 NANA -7.164039 NA bfrNA NA -1.620542 glpKNA -0.966187 NA glpRNA NA -0.481621NA NA -0.370786NA NA -0.519869NA NA -0.558052NA NA 0.4508878 gcdNA NA NA lon-2NA NA NANA NA NA lepBNA NA 0.5007856 mucBNA NA 0.280342 mucANA NA 0.5931009 rpoENA NA 4.2967204NA NA 3.2280417NA NA 2.3846269NA NA -0.897947NA NA NANA NA -1.234464 adhBNA NA NA bglXNA NA NANA NA -1.902474NA NA -1.115343NA NA -0.323748NA NA -1.983058 pcaTNA -0.472524 NANA NA -0.604711NA NA -0.761439NA -0.778112 -0.18693 hopE1NA -2.257178 NANA -1.637949 -1.041416NA NA NANA NA -0.225174NA -1.550528 NANA NA NANA NA NANA NA -0.501282NA -2.357771 -0.280977 sodB

5.819765 2.8906637 -3.395833

Page 27: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

3.1189294 2.9501298 NA2.6079728 1.1045419 -1.5883121.5948477 1.0430709 -0.787168NA NA NA colSNA NA NA colRNA -0.644481 NANA NA -1.170299 fabG1.7802479 2.6062957 NANA NA NA secANA NA NA murCNA NA NA murGNA NA NA murDNA NA NANA NA NA sspBNA -0.696102 NA sspANA NA NA rplMNA -0.726079 NA trpSNA NA 0.3228544 cysN/CNA NA NA cysDNA -0.603375 NA murANA NA NANA -0.734957 NANA -0.5009 NANA -0.815909 NANA NA NANA NA NANA NA NANA NA NANA -0.597122 NA rpoNNA NA 0.8115364NA 6.7657579 NA sodANA 7.517586 NANA 6.9373441 NA fumCNA -0.472961 NA gatCNA NA 1.070266NA NA NANA NA 0.685209 secGNA -0.940087 NA tpiANA NA NANA -2.013483 NA greANA NA 0.6466547 dapBNA -1.514788 NA dnaJNA NA NA dnaKNA NA NA grpENA NA NA recNNA -0.736438 NA omlANA NA NA smpBNA NA 1.9333553NA -0.530731 -0.518222 katGNA NA NANA -1.259692 NA garDNA NA -1.201284NA NA -1.541535NA NA -2.745063NA NA -1.091133 dppANA -2.410928 NANA -0.422131 NANA NA 0.5620218

Page 28: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA 1.9434786NA NA 2.5213387NA NA NA prfCNA 6.2774673 NANA NA -0.680931NA -1.839858 NANA NA -0.450736-1.693414 -1.97661 -0.830888 hopS2

NA -1.421445 -0.621864 shcS2NA -3.303098 NA hopS1-1.173509 -1.609763 -0.56426 shcS1

NA NA -0.756755NA 2.011325 1.4012718NA NA 1.6315049NA NA -0.86783NA NA NANA -1.002811 -0.496703 cstANA -2.589931 -1.801868NA -4.164426 -3.267371 cioBNA -4.224823 -2.527009 cioANA -0.561836 NANA NA -0.269647 cfa1NA -0.717181 NA cfa2NA NA -0.26166 cfa3NA NA -0.349803 cfa5NA NA -0.367513 cfa6NA NA NA cfa7NA NA -0.408973 cfa8NA NA NA cfa9NA -5.229542 NA hopAD1NA -2.393651 NA hopAQ1NA -2.804715 NA corRNA NA NA cmaTNA -1.346795 NANA -1.500886 NA cmaU-1.069541 -2.01319 -1.007087 hopAA1-2

NA -1.271571 -0.608966 hopV1NA -1.782808 -0.678958 shcVNA NA NANA -3.259571 -2.060749 hopG1NA -2.561408 NANA NA NANA NA -1.795079NA -0.884253 -0.775256NA -1.05818 NA hopI1NA NA NA galNA NA NANA NA NANA -0.551022 NA lipANA -0.411999 NANA NA -1.355939NA -0.580237 NA prmANA NA -0.704508NA NA NA cbpANA NA 1.2131354NA NA NANA NA NA pncBNA 2.3782144 NA azu

Page 29: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA 0.2053001 rpsFNA -0.405047 NA hflXNA NA 0.8736917 miaANA NA NA psdNA -0.826646 NANA NA -0.541921 parENA NA NANA -0.621295 NANA NA NA pilGNA -0.541447 NANA -0.587772 NANA NA NANA NA -0.643909NA NA -0.850791NA 0.973548 NA mdcANA NA -0.547233NA NA NA gltBNA -0.567757 NA hslVNA -0.563034 NA hslUNA NA NANA NA -0.636368NA NA NA hisENA NA -0.568293NA 0.5413142 NANA NA NANA -0.721661 -0.487518 cynTNA -1.347329 -0.933739NA NA 0.9312187 metI-2NA NA -0.373255NA NA NANA NA NA serANA NA -0.65882NA NA NANA NA NANA -0.784315 NANA NA NANA NA NANA NA NANA NA NANA -1.072233 NA hisHNA NA 1.719238NA -2.579072 NA shcANA -1.565908 -0.415186 hopA1NA -1.237459 NANA NA 2.2862165NA NA 3.0034822NA NA 1.339817NA NA 2.5088942NA NA 2.3561983NA NA NANA 4.3541906 NANA NA -0.315318 rfbC-2NA NA -0.520965NA NA -1.358801NA NA NANA 0.6059801 NANA 0.6246498 NANA 0.5218063 NA hcp-2

Page 30: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA -0.755919NA NA -1.210563NA NA -0.785898NA NA -1.106367NA -0.516428 NA rubBNA -0.957503 NA rubANA 0.8400172 NA aspANA NA NANA NA 1.1327752NA NA 1.056385NA NA 1.1852055NA NA NA oadANA NA NANA NA -0.637067NA -0.736604 NANA NA NANA 0.50892 NANA NA NA atpDNA NA NANA NA NANA NA NANA NA NA rnpANA -0.974053 -0.297728 plcA2NA 4.7598143 NANA NA -0.40954NA -1.157763 NANA NA NANA NA -0.629037NA NA -0.621585NA NA NANA NA -0.667917NA NA -0.683864NA NA -0.648675NA NA NA-1.001256 -1.478059 -0.628569 HopX1

NA -1.30664 NA shc01NA -0.881881 -0.525359 hopO1-1-1.229786 -1.70248 NA hopT1-10.3499072 NA -0.305373NA NA NANA 0.6090911 NA8.1394936 8.2707426 NA prrF2NA 1.5952321 NANA NA NA

Page 31: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

annotationrecombination protein Ftype I restriction-modification system, M subunit, putativeDNA-binding proteinhypothetical proteintype III effector HopK1type III effector HopY1citrate transporterhypothetical proteintonB proteinTonB system transport protein ExbDTonB system transport protein ExbBendoribonuclease L-PSP, putativeguanosine-3,5-bis(diphosphate) 3-pyrophosphohydrolaseguanylate kinasebacterial extracellular solute-binding protein, family 5aldehyde dehydrogenase family proteinD-amino acid dehydrogenase small subunitmetallo-beta-lactamase superfamily proteinATP-dependent DNA helicase Repargininosuccinate lyasetranscriptional regulator AlgQalginate regulatory protein AlgR3oligopeptidase Aosmotically inducible proteinhypothetical proteinhypothetical proteinsulfatase family proteinhypothetical proteincysteine synthasehypothetical proteinhypothetical proteinhypothetical proteinL-lysine 6-monooxygenasenitrogen regulatory protein P-IIhypothetical proteinhypothetical proteinhypothetical proteinphosphoenolpyruvate carboxykinasehypothetical proteinhypothetical proteinhypothetical proteinsulfate-binding proteinsulfate ABC transporter, permease protein CysTiron ABC transporter, periplasmic iron-binding proteinaminomethyltransferaseadenylate cyclaseglutamate--cysteine ligaseDNA-binding response regulator OmpRhypothetical proteinoxidoreductase, aldo keto reductase familyglutamine synthetase, type IGTP-binding protein TypAindoleacetate-lysine ligaseS-adenosylmethionine synthetaseglyceraldehyde-3-phosphate dehydrogenaselipoprotein, putative

: Differentially regulated genes identified at a p value less than or equal to 0.05 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 32: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

rhodanese-like domain proteinhypothetical proteinpeptidase, M16 familyRNA polymerase sigma factorsulfur carrier protein ThiSthiazole synthasebetaine aldehyde dehydrogenaseglutathione S-transferase, putativeglutathione-independent formaldehyde dehydrogenasehypothetical proteintype III chaperone protein ShcFpyrroloquinoline quinone biosynthesis protein PqqEpeptidase, M20 M25 M40 family30S ribosomal protein S21SpoVR like family proteinhypothetical proteinhypothetical proteindiadenosinetetraphosphatasehypothetical proteindimethyladenosine transferase4-hydroxythreonine-4-phosphate dehydrogenasephosphoglycolate phosphataseanthranilate synthase component Iautotransporting lipase, GDSL familytranscriptional regulator PrtN, putativebacteriocin, putativetype III effector HopH1type III effector HopC1indole-3-glycerol-phosphate synthaseS-adenosylmethionine decarboxylase proenzymehypothetical proteinhypothetical proteinN-acetyl-gamma-glutamyl-phosphate reductasehypothetical proteintyrosyl-tRNA synthetasetranslocasetranscription antitermination protein NusG50S ribosomal protein L1150S ribosomal protein L150S ribosomal protein L1050S ribosomal protein L7 L1230S ribosomal protein S1230S ribosomal protein S730S ribosomal protein S1050S ribosomal protein L350S ribosomal protein L2350S ribosomal protein L2230S ribosomal protein S350S ribosomal protein L2450S ribosomal protein L530S ribosomal protein S1450S ribosomal protein L1850S ribosomal protein L3050S ribosomal protein L3630S ribosomal protein S1330S ribosomal protein S11DNA-directed RNA polymerase alpha subunitbacterioferritin

Page 33: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

major facilitator family transporterlipopolysaccharide biosynthesis protein, putativeouter membrane protein OmpWlipoprotein, putativeriboflavin synthase subunit alphaexodeoxyribonuclease VII small subunitglutathione S-transferase family proteinethanolamine ammonia-lyase, heavy subunitaldehyde dehydrogenase family proteiniron(III) dicitrate transport system, periplasmic iron-binding protein FecBexodeoxyribonuclease V, gamma subunitexodeoxyribonuclease V, beta subunitexodeoxyribonuclease V, alpha subunitoctylprenyl diphosphate synthase50S ribosomal protein L21GTP-binding protein, GTP1 Obg familyhypothetical proteinisoleucyl-tRNA synthetasepeptidyl-prolyl cis-trans isomerase, FKBP-typeclpB proteinalcohol dehydrogenase, zinc-containingribD C-terminal domain proteinhypothetical proteinhypothetical proteinmajor facilitator family transporterhypothetical proteintype III effector HopAJ1PSPTO5621dnaK suppressor protein, putativeParA family proteinhypothetical proteinmacrolide efflux protein, putativeamidinotransferase family proteinnikkomycin biosynthesis domain proteinhypothetical proteintype III effector HopD1type III effector HopQ1-1type III effector HopR1methyl-accepting chemotaxis proteintype IV pilus biogenesis proteinglutathione S-transferasetellurium resistance protein TerZtellurium resistance protein TerDtellurium resistance protein TerEtellurium resistance protein, putativephosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components1-phosphofructokinaseglucose-6-phosphate isomerasepantoate--beta-alanine ligase3-methyl-2-oxobutanoate hydroxymethyltransferasepentapeptide repeat domain proteinhypothetical proteinhypothetical proteinhypothetical proteincarbonic anhydraseGDP-mannose 4,6-dehydratasehypothetical proteinDnaJ domain protein

Page 34: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

hypothetical proteinlipopolysaccharide biosynthesis proteinO-antigen ABC transporter, ATP-binding protein, putativedTDP-4-dehydrorhamnose reductasepeptidyl-tRNA hydrolaseribose-phosphate pyrophosphokinaseamino acid ABC transporter, periplasmic amino acid-binding proteinmalate:quinone oxidoreductaselipoprotein, putativeacyl-CoA synthasehypothetical proteinompA family proteinhypothetical proteinGTP cyclohydrolase Ihypothetical proteinregulatory protein, putativehypothetical proteintranscriptional regulator, AraC familymembrane proteinPhoH-like proteinamino acid ABC transporter, ATP-binding proteinDNA-binding protein HU familyglycine cleavage system T proteinglycine dehydrogenasehypothetical proteinheme oxygenase, putativeTonB-dependent outer membrane heme receptorglyceraldehyde-3-phosphate dehydrogenasephosphogluconate dehydrataseglucokinaseDNA-binding response regulatorglucose ABC transporter, periplasmic glucose-binding protein, putativeglucose ABC transporter, ATP-binding proteinporin BHex regulon repressorglucose-6-phosphate 1-dehydrogenase6-phosphogluconolactonaseketo-hydroxyglutarate-aldolase keto-deoxy- phosphogluconate aldolasehypothetical proteincarbonic anhydraseconserved effector locus proteintype III effector HopN1conserved effector locus proteintype III effector HopAA1-1type III helper protein HrpW1type III chaperone ShcMtype III effector HopM1type III effector protein AvrE1membrane-bound lytic murein transglycosylase D, putativetype III transcriptional regulator HrpRtype III transcriptional regulator HrpStype III helper protein HrpA1type III helper protein HrpZ1type III secretion protein HrpB(Pto)type III secretion protein HrcJtype III secretion protein HrpDtype III secretion protein HrpEtype III secretion protein HrpF

Page 35: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

type III secretion protein HrpGouter-membrane type III secretion protein HrcCtype III secretion protein HrpTnegative regulator of hrp expression HrpVtype III secretion protein HrcStype III secretion protein HrcRtype III secretion protein HrcQbtype III secretion protein HrcQatype III secretion protein HrpPtype III secretion protein HrpOtype III secretion cytoplasmic ATPase HrcNtype III secretion protein HrpQtype III secretion protein HrcVtype III secretion protein HrpJRNA polymerase sigma factor HrpLtype III helper protein HrpK1type III effector HopB1PSPTO5622hypothetical proteinhypothetical proteinpreprotein translocase subunit YajCrrf2 family proteincysteine desulfurasehypothetical proteinradical SAM enzyme, Cfr familycarboxyphosphonoenolpyruvate phosphonomutasehypothetical proteinmulticopper oxidase5 -phosphoribosylglycinamide transformylasesignal recognition particle protein Ffh30S ribosomal protein S1616S rRNA-processing proteintRNA (guanine-N(1)-)-methyltransferasethiol:disulfide interchange protein DsbCompA family proteinhypothetical proteinphosphoenolpyruvate carboxylaseadenylate kinasearsC family proteinPII uridylyl-transferasephosphatidate cytidylyltransferasemembrane-associated zinc metalloprotease, putativeouter membrane protein OmpH, putativeUDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase(3R)-hydroxymyristoyl ACP dehydrataseUDP-N-acetylglucosamine acyltransferaselipid-A-disaccharide synthaseribonuclease HIIDNA polymerase III subunit alphaacetyl-CoA carboxylase alpha subunitstationary phase survival protein SurEprotein-L-isoaspartate O-methyltransferaseRNA polymerase sigma factortype III effector HopAF1PSPTO5620hypothetical proteinhypothetical proteinacetyltransferase, GNAT family

Page 36: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

asparagine synthetase, glutamine-hydrolyzingLysM domain proteinaerotaxis receptorhypothetical proteinarsenate reductasehypothetical proteinMazG family proteinphosphoribosylglycinamide formyltransferasecob(I)yrinic acid a,c-diamide adenosyltransferaseglutathione peroxidase family proteinouter membrane proteinhypothetical proteinhypothetical proteinhypothetical proteinhypothetical proteinshort chain dehydrogenaseDNA gyrase subunit Acytidylate kinasehypothetical proteinhypothetical proteinheat shock protein HtpXaspartate aminotransferasenitroreductase family proteinputative intracellular septation proteinaromatic amino acid permeaseriboflavin synthase subunit betaaspartate kinaseTonB-dependent receptor, putativeL-serine dehydratase 1piperideine-6-carboxylate dehydrogenasebacteriophytochrome histidine kinase3-oxoacyl-(acyl-carrier-protein) synthase III, putativecyanate hydrataseflagellar basal body rod proteinflagellar hook proteinflagellar basal-body rod protein FlgF3-oxoacyl-(acyl-carrier-protein) synthase III, putativeflagellinflagellin FlaG, putativeflagellar hook-associated protein FliDflagellar biosynthesis proteinflagellar biosynthesis sigma factor FliAaconitate hydratasehypothetical proteinGTP cyclohydrolase IHAD-superfamily hydrolasehypothetical proteinhypothetical proteinhypothetical proteinhelicase SNF2 family domain proteinglyceraldehyde-3-phosphate dehydrogenasemajor facilitator family transporterthiamine biosynthesis lipoprotein, putativeGTP cyclohydrolase I, putativehypothetical proteinresponse regulatorDNA-binding response regulator, LuxR familyRNA polymerase sigma-70 factor

Page 37: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

pyoverdine synthetase, thioesterase componentpeptide synthasediaminobutyrate--2-oxoglutarate aminotransferaseMbtH-like proteinABC transporter, periplasmic substrate-binding protein, putativecation ABC transporter, permease proteincation ABC transporter, periplasmic cation-binding proteinhypothetical proteinhypothetical proteinhypothetical proteiniron-regulated membrane protein, putativepyoverdine biosynthesis regulatory gene, putativepyoverdine sidechain peptide synthetase I, epsilon-Lys modulepyoverdine sidechain peptide synthetase II, D-Asp-L-Thr componentpyoverdine sidechain peptide synthetase III, L-Thr-L-Ser componentpyoverdine sidechain peptide synthetase IV, D-Asp-L-Ser componentTonB-dependent siderophore receptor, putativepyoverdine ABC transporter, ATP-binding permease proteinhypothetical proteinaminotransferase, class Vrenal dipeptidase family proteinefflux transporter, RND family, MFP subunitpenicillin amidase family proteintranscriptional regulator, LysR familyisopropylmalate isomerase large subunitisopropylmalate isomerase small subunit3-isopropylmalate dehydrogenaseaspartate-semialdehyde dehydrogenasemandelate racemase muconate lactonizing enzyme family proteinelectron transfer flavoprotein, alpha subunithypothetical proteinsuccinate dehydrogenase, cytochrome b556 subunitsuccinate dehydrogenase, hydrophobic membrane anchor proteinsuccinate dehydrogenasesuccinate dehydrogenase catalytic subunitsuccinyl-CoA synthetase subunit betaheat shock protein 903-hydroxydecanoyl-ACP dehydratasemethyl-accepting chemotaxis proteinhypothetical protein3-deoxy-7-phosphoheptulonate synthasephosphoadenosine phosphosulfate reductasehydrolase, haloacid dehalogenase-like familyRNA polymerase sigma-70 factorribosome modulation factor-related proteindeoxyguanosinetriphosphate triphosphohydrolaseprotocatechuate 3,4-dioxygenase, beta subunitprotocatechuate 3,4-dioxygenase, alpha subunit3-carboxy-cis,cis-muconate cycloisomerase4-hydroxyphenylpyruvate dioxygenase, putativeribose ABC transporter, periplasmic ribose-binding proteinribose ABC transporter proteininosine uridine-preferring nucleoside hydrolasehypothetical proteintranslation initiation factor IF-350S ribosomal protein L3550S ribosomal protein L20phenylalanyl-tRNA synthetase alpha subunit

Page 38: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

hypothetical proteinlipoprotein, putativehypothetical proteinsalicylate biosynthesis isochorismate synthasechorismate mutaseyersiniabactin synthetase, salycilate ligase componentyersiniabactin synthetase, thioesterase componentyersiniabactin synthetase, thiazolinyl reductase componentyersiniabactin polyketide non-ribosomal peptide synthetasehypothetical proteinyersiniabactin non-ribosomal peptide synthetaseABC transporter, ATP-binding permease proteinABC transporter, ATP-binding permease proteinTonB-dependent siderophore receptor, putativeSco1 SenC family proteinL-arabinose ABC transporter, periplasmic L-arabinose-binding proteintype III helper protein HopP1succinate-semialdehyde dehydrogenasemembrane protein, TerC familyfructokinasexylulokinaseD-mannonate oxidoreductasemannitol ABC transporter, permease proteinmannitol ABC transporter, periplasmic mannitol-binding proteinprotein-glutamate methylesterase, putativeenoyl-CoA hydrataseNADH pyrophosphatasehypothetical proteinsulphite reductase5-methyltetrahydrofolate--homocysteine methyltransferasethiol peroxidaselipoprotein, putativehypothetical proteindienelactone hydrolase family proteinnon-ribosomal peptide synthetasehypothetical proteinhypothetical proteinTonB-dependent siderophore receptor, putativecytochrome c family proteinhypothetical proteinSCO1 SenC family proteinhypothetical proteinTonB-dependent receptor, putativehypothetical proteintype III effector HopL1hypothetical proteinhypothetical proteinlipoprotein, putativevanillate O-demethylase, oxygenase subunitalcohol dehydrogenase, zinc-containinghypothetical proteintype III effector HopAB2hypothetical proteinalkyl hydroperoxide reductase, subunit Chypothetical proteinCof-like hydrolase family proteinglucose-6-phosphate 1-dehydrogenase6-phosphogluconate dehydrogenase

Page 39: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

glycogen operon protein GlgXacyl carrier protein phosphodiesterasecobalamin synthesis protein P47K family proteinhypothetical proteinhypothetical proteinhypothetical proteinenoyl-CoA hydratase isomerase family proteinacetyl-CoA acetyltransferasePqiB family proteinsensor histidine kinasephosphate ABC transporter, periplasmic phosphate-binding proteinhypothetical proteinlipoprotein, putativemethyl-accepting chemotaxis proteinTonB-dependent siderophore receptor, putativealdehyde dehydrogenase family proteinprotease inhibitor Inhhypothetical proteinhypothetical proteincell division protein FtsKtranslation initiation factor IF-1ATP-dependent clp protease, ATP-binding subunit ClpAcold shock domain family proteinhypothetical proteinisocitrate lyaseNADH dehydrogenase alpha subunitNADH dehydrogenase beta subunitNADH dehydrogenase I, C D subunitATP synthase subunit ENADH dehydrogenase I, F subunitNADH dehydrogenase gamma subunitNADH dehydrogenase subunit HNADH dehydrogenase subunit JNADH dehydrogenase subunit MNADH dehydrogenase subunit Nsensor histidine kinaseDNA-binding response regulatorlipoprotein, putativehypothetical protein6-pyruvoyl tetrahydrobiopterin synthase, putative3-oxoacid CoA-transferase, subunit A familyTonB-dependent siderophore receptorhypothetical proteindnaK suppressor protein, putativeiolH proteinmyo-inositol 2-dehydrogenaseiolD proteiniolB proteinLexA repressorDNA topoisomerase Ifatty oxidation complex, alpha subunituniversal stress protein familyhypothetical proteinhypothetical proteinfumarylacetoacetasehomogentisate 1,2-dioxygenase4-hydroxyphenylpyruvate dioxygenasemaleylacetoacetate isomerase

Page 40: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

TonB-dependent siderophore receptor, putativemethyl-accepting chemotaxis proteinmethyl-accepting chemotaxis proteincatalasehypothetical proteinhypothetical proteindyp-type peroxidase family proteinhypothetical proteinhypothetical proteinhypothetical proteinDNA polymerase III subunits gamma and tauhypothetical proteinhypothetical proteinhypothetical proteinTonB-dependent siderophore receptoroxidoreductase, aldo keto reductase familyenoly-CoA hydratase isomerase family proteinacyl-CoA dehydrogenaseDNA polymerase III subunit epsilonribonuclease Hhypothetical proteinmembrane-bound lytic murein transglycosylase DABC transporter, permease proteinenoyl-(acyl-carrier-protein) reductasetrigger factormethylenetetrahydrofolate dehydrogenase methenyltetrahydrofolate cycaconitate hydratasehypothetical proteinhypothetical proteinhypothetical proteinaminopeptidase Nhypothetical proteinacetyl-CoA carboxylase beta subunittype IV pilus biogenesis protein PilZ3-oxoacyl-(acyl carrier protein) synthaseacyl-carrier-protein S-malonyltransferasefatty acid phospholipid synthesis proteinhypothetical proteinautoinducer synthesis protein PsyIseptum formation inhibitorABC transporter, periplasmic substrate-binding proteinglyoxalase, putativecysteine synthase Ahypothetical proteingas vesicle protein, putativephosphoribosylaminoimidazole-succinocarboxamidesynthasemetallo-beta-lactamase superfamily proteinhypothetical proteinAhpC Tsa family proteinquinolinate synthetasetranslocation protein TolB precursortolA proteintolR proteintolQ proteinhypothetical proteinDps family proteincold shock domain family proteinporin D

Page 41: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

type III effector protein AvrPto1repressor protein cIhypothetical proteinferredoxin--NADP reductaseDNA-binding response regulator, LuxR familyrecombinase AferredoxinMaoC-like domain proteintype III effector HopAK1hypothetical proteinhigh-affinity branched-chain amino acid ABC transporter, periplasmic amiamino acid ABC transporter, periplasmic amino acid-binding proteincold shock protein CapBmethionyl-tRNA synthetaseargininosuccinate synthasedihydroorotaseribonuclease Tbacterioferritin-associated ferredoxinbacterioferritinglycerol kinaseglycerol-3-phosphate regulon repressoramino acid ABC transporter, periplasmic amino acid-binding proteinamino acid ABC transporter, permease proteinamino acid ABC transporter, permease proteinamino acid ABC transporter, ATP-binding proteinglucose dehydrogenaseATP-dependent protease Lahypothetical proteinsignal peptidase Isigma factor algU regulatory protein MucBsigma factor algU negative regulatory protein MucARNA polymerase sigma-70 factorTctC protein, putativemembrane protein TctB, putativemembrane protein TctA, putativeDNA-binding proteinacetyltransferase, GNAT familyalcohol dehydrogenase IIbeta-glucosidasemetabolite-proton symporter, putativehypothetical proteinhypothetical proteinouter membrane efflux proteindicarboxylic acid transport proteinphosphate transporter family proteinhypothetical proteinhypothetical proteintype III effector HopE1hypothetical proteinmoxR protein, putativehypothetical proteinhypothetical proteinfumarate hydratase, class I, putativeinsecticidal toxin protein, putativetranscriptional regulator, ArsR familyoxidoreductase, FAD FMN-bindingsuperoxide dismutase, Feiron-regulated protein A, putative

Page 42: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

lipoprotein, putativelipoprotein, putativelipoprotein, putativesensor histidine kinase ColSDNA-binding response regulator ColRcytoplasmic membrane family protein3-ketoacyl-(acyl-carrier-protein) reductasehypothetical proteintranslocaseUDP-N-acetylmuramate--L-alanine ligaseN-acetylglucosaminyl transferaseUDP-N-acetylmuramoyl-L-alanyl-D-glutamatesynthetasehypothetical proteinstringent starvation protein Bstringent starvation protein A50S ribosomal protein L13tryptophanyl-tRNA synthetasebinfunctional sulfate adenylyltransferase subunit 1 adenylylsulfate kinasesulfate adenylyltransferase subunit 2UDP-N-acetylglucosamine 1-carboxyvinyltransferasetoluene tolerance protein, putativeSTAS domain proteintoluene tolerance protein, putativemce-related proteinhypothetical proteinhypothetical proteinostA family proteinABC transporter, ATP-binding proteinDNA-directed RNA polymerase subunit Nhypothetical proteinsuperoxide dismutase, Mnhypothetical proteinfumarate hydrataseaspartyl glutamyl-tRNA amidotransferase subunit Chypothetical proteinhypothetical proteinpreprotein translocase, SecG subunittriosephosphate isomerasehypothetical proteintranscription elongation factor GreAdihydrodipicolinate reductasednaJ proteinmolecular chaperone DnaKheat shock protein GrpEDNA repair protein RecNouter membrane lipoprotein OmlASsrA-binding proteinhypothetical proteincatalase peroxidase HPIGAF domain GGDEF domain EAL domain proteinD-galactarate dehydratasepeptide ABC transporter, periplasmic peptide-binding proteindipeptide ABC transporter, periplasmic dipeptide-binding protein, putativouter membrane porin, OprD familydipeptide ABC transporter, periplasmic dipeptide-binding proteindipeptide ABC transporter, permease proteinhypothetical proteinglycine betaine carnitine choline ABC transporter, ATP-binding protein

Page 43: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

glycine betaine L-proline ABC transporter, periplasmic substrate-binding proteinglycine betaine carnitine choline ABC transporter, permease proteinpeptide chain release factor 3hypothetical proteinhypothetical proteinhypothetical proteinATP-dependent protease, putativetype III effector HopS2type III chaperone ShcS2type III effector HopS1type III chaperone ShcS1hypothetical proteinhypothetical proteinhypothetical proteintranscriptional regulator, LysR familyC4-dicarboxylate transporter malic acid transport proteincarbon starvation protein CstAhypothetical proteincyanide-insensitive terminal oxidase CioBcyanide-insensitive terminal oxidase CioAhypothetical proteincoronafacic acid synthetase, acyl carrier protein componentcoronafacic acid synthetase, dehydratase componentcoronafacic acid beta-ketoacyl synthetase componentcoronafacic acid synthetase, ligase componentcoronafacic acid polyketide synthase Icoronafacic acid polyketide synthetase IIcrotonyl-CoA reductaseCFA synthetase, thioesterase componenttype III effector HopAD1type III effector HopAQ1DNA-binding response regulator CorRcoronamic acid synthetase, thioesterase componentalanyl tRNA synthetase-related proteincmaU proteintype III effector HopAA1-2type III effector HopV1type III chaperone ShcVhypothetical proteintype III effector HopG1hypothetical proteinhypothetical proteinvon Willebrand factor type A domain proteinhypothetical proteintype III effector HopI1D-galactose 1-dehydrogenasePhoH-like proteinmetal ion transporter, putativelipoyl synthaselipoprotein, rlpA familyhypothetical proteinribosomal protein L11 methyltransferasephosphinothricin N-acetyltransferase, putativecurved-DNA-binding proteinosmotically-inducible lipoprotein OsmE, putativehigh affinity branched-chain amino acid ABC transporter, periplasmic amino acid-binding proteinnicotinate phosphoribosyltransferaseazurin

Page 44: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

30S ribosomal protein S6GTP-binding protein HflXtRNA delta(2)-isopentenylpyrophosphate transferasephosphatidylserine decarboxylasehypothetical proteinDNA topoisomerase IV subunit Blipopolysaccharide biosynthesis protein RfaEcarbamoyltransferase family proteintype IV pilus response regulator PilGhypothetical proteinYGGT family proteinhomoserine O-acetyltransferasehypothetical proteincytochrome b561, putativemalonate decarboxylase, alpha subunitParA family proteinglutamate synthase, large subunitATP-dependent protease peptidase subunitATP-dependent protease ATP-binding subunithypothetical proteinpolyhydroxyalkanoate granule-associated protein PhaFphosphoribosyl-ATP pyrophosphatasehypothetical proteinhypothetical proteinhypothetical proteincarbonic anhydrasesulfate transporter family proteinD-methionine ABC transporter, permease proteinfumarylacetoacetate hydrolase family proteinoxidoreductase, FAD-bindingD-3-phosphoglycerate dehydrogenaseglutamine synthetaseglutamine synthetaseouter membrane porin, OprD familyglutaredoxinrhodanese-like domain proteinpeptidase, M23 M37 familycarboxyl-terminal protease family proteinhypothetical proteinimidazole glycerol phosphate synthase subunit HisHlipoprotein, putativetype III chaperone protein ShcAtype III effector HopA1hypothetical proteinhypothetical proteinhypothetical proteinhypothetical proteinallophanate hydrolase, putativebiotin carboxylase biotin carboxyl carrier proteinhypothetical proteinhypothetical proteindTDP-4-dehydrorhamnose 3,5-epimerasemutT nudix family proteinoxidoreductase, molybdopterin-bindingFHA domain proteinhypothetical proteinhypothetical proteinsecreted protein Hcp

Page 45: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

HAD-superfamily hydrolaseoxidoreductase, aldo keto reductase familyhypothetical proteinDNA-binding protein HU familyrubredoxin reductaserubredoxinaspartate ammonia-lyasesodium alanine transportertranscriptional regulator, putativeacetyltransferase, GNAT familyacetyltransferase, GNAT familyoxaloacetate decarboxylaseacetyl-CoA carboxylasehypothetical proteincytosolic long-chain acyl-CoA thioester hydrolase family proteinhypothetical proteinhypothetical proteinATP synthase subunit BParB family proteinParA family proteinhypothetical proteinribonuclease Pphosphoesterase family proteinPilM protein, putativemajor facilitator family transporterhypothetical proteinhypothetical proteinhypothetical proteinhypothetical proteinsurface exclusion protein, putativehypothetical proteinpartion protein, ParB familyATPase, ParA familyresolvase, putativetype III effector HopX1type III chaperone ShcO1type III effector HopO1-1type III effector HopT1-1hypothetical proteinhypothetical proteinwithin intergenic region 555256-555670within intergenic region 3549362-3549773within intergenic region 3679906-3680084within intergenic region 6038188-6038782

Page 46: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

notesRequired for DNA replication; binds preferentially to single-stranded, linear DNA

identified by match to PFAM protein family HMM PF01381identified by Glimmer2; putativepreviously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putativePreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF04073similar to GP:14595286, and GP:14595286; identified by sequence similarity; putativesimilar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putativesimilar to GP:14595284; identified by sequence similarity; putativesimilar to GB:L19158, GB:D26443, GB:U03504, GB:Z31713, SP:P43003, PID:487339, PID:607113, PID:825504, and PID:825663; identified by sequence similarity; putativesimilar to GP:9951657, and SP:P17580; identified by sequence similarity; putativeEssential for recycling GMP and indirectly, cGMPidentified by match to PFAM protein family HMM PF00496similar to SP:P23883, GB:M11147, GB:M10119, GB:M12938, GB:X03742, GB:X03743, SP:P02792, PID:1340145, PID:1340146, PID:182514, PID:182516, PID:182518, PID:2230869, and PID:28519; identified by sequence similarity; putativecatalyzes the oxidative deamination of D-amino acidssimilar to GP:12721862; identified by sequence similarity; putativesimilar to SP:P09980; identified by sequence similarity; putativecatalyzes the formation of arginine from (N-L-arginino)succinate

similar to SP:P27298; identified by sequence similarity; putativesimilar to SP:P23929, GB:M16447, GB:X04882, SP:P09417, PID:181553, and PID:30819; identified by sequence similarity; putativesimilar to GP:9945860; identified by sequence similarity; putativesimilar to GP:15978663; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00884identified by Glimmer2; putativesimilar to GP:12082815, and SP:P37887; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by match to TIGR protein family HMM TIGR00950similar to SP:P11295; identified by sequence similarity; putativesimilar to GP:2735324; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00149identified by Glimmer2; putative

PEP carboxykinase; PEP carboxylase; PEPCK; catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using ATPsimilar to GP:19915183; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to SP:P33159, GB:X68014, and PID:40807; identified by sequence similarity; putativesimilar to SP:P06997, GB:M25322, GB:M60218, GB:M60219, GB:M60222, GB:M60223, GB:M60224, GB:M60225, GB:M60226, GB:M60227, GB:M60228, GB:M60229, GB:M60230, GB:M60231, GB:M60232, GB:M60233, GB:M60234, GB:M60235, SP:P16109, PID:183389, and PID:183391; identified by sequence similarity; putative

catalyzes the formation of dihydrolipoylprotein from S-aminomethyldihydrolipoprotein in the glycine cleavage systemidentified by match to PFAM protein family HMM PF01928Involved in the first step of glutathione biosynthesis

similar to SP:Q9HT89; identified by sequence similarity; putativesimilar to SP:Q46851, GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01692identified by match to PFAM protein family HMM PF03144similar to SP:P18204, GB:J04031, SP:P11586, and PID:307178; identified by sequence similarity; putativemethionine adenosyltransferase; catalyzes the formation of S-adenosylmethionine from methionine and ATPcatalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphate

: Differentially regulated genes identified at a p value less than or equal to 0.05 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 47: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:2661707; identified by sequence similarity; putativesimilar to SP:P22539, GB:M60111, GB:X59593, PID:147848, PID:396397, PID:42975, GB:U00096, and PID:1790497; identified by sequence similarity; putativesimilar to GP:9946224; identified by sequence similarity; putativeBinds with the catalytic core of RNA polymerase to produce the holoenzymewith ThiF, ThiG, and ThiO catalyzes the formation of the thiazole moiety of thiamine pyrophosphateCatalyzes the formation of thiazole from glycine imine, 1-deoxy-D-xylulose-5-phosphate and ThiS-thiocarboxylate

similar to SP:P32105; identified by sequence similarity; putativesimilar to SP:P46154, GB:X64318, GB:U26173, GB:S79880, PID:1237118, and PID:30956; identified by sequence similarity; putativesimilar to GP:9946369, and GP:9946369; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF01546Interacts with residues in the 16S gene, protecting the stem-loop structureidentified by match to PFAM protein family HMM PF04293identified by match to PFAM protein family HMM PF04285similar to SP:P77391; identified by sequence similarity; putativeCatalyzes the hydrolysis of P1,P4-bis(5 -adenosyl) tetraphosphate

Catalyzes the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases in 16S rRNAAn essential cofactor for many enzymes responsible for the metabolic conversions of amino acidsCatalyzes the conversion of 2-phosphoglycolate to glycolate and phosphatecatalyzes the formation of anthranilate and glutamate from chorismate and glutamine

similar to SP:P05820; identified by sequence similarity; putativepreviously known as HopPtoH (PMID 12032338; Petnicki-Ocwieja et al, 2002).previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586Catalyzes the conversion of 1-(2-carboxyphenylamino)1-deoxy-D-ribulose 5 phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate during the biopsynthesis of tryptophanS-adenosylmethionine provides the aminopropyl moiety required for spermidine biosynthesis from putrescineidentified by match to PFAM protein family HMM PF04241

catalyzes the reduction of N-acetyl-5-glutamyl phosohate to N-acetyl-glutamate 5-semialdehyde in arginine biosynthesisidentified by match to PFAM protein family HMM PF03702catalyzes the formation of tyrosyl-tRNA(Tyr) from tyrosine and tRNA(Tyr)

Modulates Rho-dependent transcription terminationbinds directly to 23S ribosomal RNABinds directly to 23S rRNA and is located proximal to the site where elongation factor Tu is bound to the ribosomebinds the two ribosomal protein L7/L12 dimers and anchors them to the large ribosomal subunitpresent in two forms; L12 is normal, while L7 is aminoacylated at the N-terminal serine; the only multicopy ribosomal protein; 4:1 ratio of L7/L12 per ribosome; two L12 dimers bind L10; critically important for translation efficiency and fidelity; stimulatImportant for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S sOne of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding centerInvolved in the binding of tRNA to the ribosomesBinds directly near the 3 end of the 23S rRNA, where it nucleates assembly of the 50S subunitBinds signal recoginition particle and trigger factor at the peptide exit area on the 50S ribosomeBinds specifically to 23S rRNA during the early stages of 50S assembly. It makes multiple contacts with different domains of te 23S rRNA in the assembled 50S subunit and ribosomeforms a complex with S10 and S14; binds the lower part of the 30S subunit head and the mRNA in the complete ribosome to position it for translationFound in the ribonucleoprotein core and is involved in the early assembly of the 50S subunitMediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberancelocated in the peptidyl transferase center and involved in assembly of 30S ribosome subunitbinds 5S rRNANon-essential, may be involved in procession of translationRibosomal protein L36 is the smallest protein from the large subunit of the prokaryotic ribosomeLocated at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNAlocated on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosomeCatalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

Page 48: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazinecatalyzes the bidirectional exonucleolytic cleavage of DNAsimilar to GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putativesimilar to SP:P08394; identified by sequence similarity; putativesimilar to GP:3142727, and SP:P04993; identified by sequence similarity; putative

catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile)

identified by match to TIGR protein family HMM TIGR01751similar to GB:S69136, GB:S69198, GB:M28594, and PID:292763; identified by sequence similarity; putativeAlso known as ORF24 (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to TIGR protein family HMM TIGR01449identified by Glimmer2; putativesimilar to GB:U01783, and PID:409855; identified by sequence similarity; putativesimilar to SP:P77262; identified by sequence similarity; putativepreviously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putativeIdentified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.similar to SP:P18274, GB:M25499, SP:P16588, and PID:155251; identified by sequence similarity; putativesimilar to PIR:B42465; identified by sequence similarity; putativesimilar to GP:20520259; identified by sequence similarity; putativesimilar to GP:6683463, and GP:14578840; identified by sequence similarity; putativesimilar to GP:5919222, GB:M13699, GB:D00025, GB:X69706, GB:M13536, GB:X04136, GB:X04137, GB:X04138, SP:P00450, PID:1335036, PID:1335037, PID:1666064, and PID:180249; identified by sequence similarity; putativesimilar to GP:14030855; identified by sequence similarity; putativeAlso known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putativesimilar to GP:4235392; identified by sequence similarity; putative

similar to SP:P39100; identified by sequence similarity; putativesimilar to SP:Q52353; identified by sequence similarity; putativesimilar to SP:P18781; identified by sequence similarity; putativesimilar to SP:P18782; identified by sequence similarity; putativesimilar to GP:4837634, GB:J02958, GB:M35074, GB:X54559, GB:U11813, GB:M35073, SP:P08581, PID:307196, PID:386868, PID:487742, PID:530800, and PID:625086; identified by sequence similarity; putative

phosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components

catalyzes the formation of D-fructose 6-phosphate from D-glucose 6-phosphateCatalyzes the formation of (R)-pantothenate from pantoate and beta-alanineCatalyzes the first committed step in the biosynthesis of pantothenateidentified by match to PFAM protein family HMM PF00805similar to GP:9950959; identified by sequence similarity; putativesimilar to GP:9950957, and GP:9950957; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF04288similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putativesimilar to GP:14090400; identified by sequence similarity; putativesimilar to GP:15141291, and GP:10719751; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00226

Page 49: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:14090397; identified by sequence similarity; putativesimilar to GP:2558982, and GP:14090396; identified by sequence similarity; putativesimilar to GP:3142220, GB:X04409, GB:X56009, GB:M21139, GB:M21740, GB:M21140, GB:M21741, GB:M21141, GB:M21142, GB:X04408, GB:X07036, GB:M14631, GB:U12466, SP:P04895, PID:31913, PID:386745, PID:386746, and PID:527671; identified by sequence similarity; putative

Enables the recycling of peptidyl-tRNAs produced at termination of translationcatalyzes the formation of 5-phospho-alpha-D-ribose 1-phosphate from D-ribose 5-phosphate and ATP

identified by match to PFAM protein family HMM PF01435Activates fatty acids by binding to coenzyme Aidentified by Glimmer2; putativesimilar to GP:5123490; identified by sequence similarity; putativesimilar to GP:19071498, and GP:19071498; identified by sequence similarity; putativeinvolved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymersimilar to GB:M60091, GB:L46359, GB:L46360, GB:L46361, GB:L46362, GB:L48713, GB:L48715, GB:L48716, SP:P07902, PID:1066737, PID:1066749, PID:1066751, PID:1066753, PID:182951, PID:306759, PID:950351, PID:950353, PID:950355, PID:950357, PID:950365, PID:950367, PID:950369, PID:950377, PID:950381, PID:950383, PID:950391, PID:950393, PID:950395, PID:950397, PID:950399, PID:950401, PID:950403, and PID:950405; identified by sequence similarity; putative

similar to GP:13936369; identified by sequence similarity; putativesimilar to GP:13936368; identified by sequence similarity; putative

acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine

catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphatecatalyzes the formation of 2-dehydro-3-deoxy-6-phospho-D-gluconate from 6-phospho-D-gluconatecatalyzes the conversion of ATP and D-glucose to ADP and D-glucose 6-phosphate

catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphatecatalyzes the formation of 6-phospho-D-gluconate from 6-phospho-D-glucono-1,5-lactonecatalyzes the formation of pyruvate and glyoxylate from 4-hydroxy-2-oxoglutarate; or pyruvate and D-glyceraldehyde 3-phosphate from 2-dehydro-3-deoxy-D-glyconate 6-phosphate

identified by match to TIGR protein family HMM TIGR01409similar to GP:8037800; identified by sequence similarity; putativeAlso known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586similar to GP:8037798, SP:P32109, GB:U15124, and PID:563996; identified by sequence similarity; putativepreviously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987similar to GP:3694999, and GP:8037796; identified by sequence similarity; putative

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putativesimilar to SP:P23931; identified by sequence similarity; putativesimilar to GB:X74863, SP:P52954, PID:1617116, and PID:510998; identified by sequence similarity; putativesimilar to GP:639829, and GP:639829; identified by sequence similarity; putativesimilar to GP:790907; identified by sequence similarity; putativesimilar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3603316, and GP:9800449; identified by sequence similarity; putativesimilar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3228545, GB:U09067, PID:483876, and PID:553456; identified by sequence similarity; putative

Page 50: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:3603319, and GP:3228546; identified by sequence similarity; putativesimilar to GP:3228547, GB:M96789, SP:P35212, and PID:183223; identified by sequence similarity; putativesimilar to GP:3603321, and GP:3603255; identified by sequence similarity; putativesimilar to GP:3603256, and GP:3228549; identified by sequence similarity; putativesimilar to GP:3282782, and GP:11276517; identified by sequence similarity; putativesimilar to GP:11276516; identified by sequence similarity; putativesimilar to GP:11276515, and GP:11276515; identified by sequence similarity; putativesimilar to GP:3282779, and GP:11276514; identified by sequence similarity; putativesimilar to GP:11276513, GB:L22846, SP:Q14209, and PID:410207; identified by sequence similarity; putativesimilar to GP:3282777, and GP:11276512; identified by sequence similarity; putativesimilar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putativesimilar to GP:11276510; identified by sequence similarity; putativesimilar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putativesimilar to GP:5360281, and SP:P37929; identified by sequence similarity; putativesimilar to GP:8037778, and GP:8037778; identified by sequence similarity; putativeAlso known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

identified by Glimmer2; putativesimilar to GP:15980288; identified by sequence similarity; putativemember of preprotein translocase; forms a heterotrimer with SecD and SecF; links the SecD/SecF/YajC/YidC complex with the SecY/SecE/SecG complex

Catalyzes the pyridoxal phosphate-dependent desulfuration of L-cysteine

similar to GP:47149, and SP:P11435; identified by sequence similarity; putativesimilar to GP:17982579; identified by sequence similarity; putative

Involved in de novo purine biosynthesis

A magnesium-dependent DNase which introduces nicks into supercoiled DNA moleculesEssential for efficient processing of 16S rRNAmethylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNA

catalyzes the formation of oxaloacetae from phosphoenolpyruvateessential enzyme that recycles AMP in active cells; converts ATP and AMP to two molecules of ADP

Catalyzes the uridylylation or deuridylylation of the PII nitrogen regulatory protein

adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesisin Pseudomonas aeruginosa this enzyme is a trimer of dimers; essential for membrane formation; performs third step of type II fatty acid biosynthesis; catalyzes dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACPcatalyzes the addition of (R)-3-hydroxytetradecanoyl to the glucosamine disaccharide in lipid A biosynthesiscatalyzes the formation of lipid A disaccharide from UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate; lipid A disaccharide is a precursor of lipid A that anchors LPS to the OMRNH2; RNase HII; binds manganese; endonuclease which specifically degrades the RNA of RNA-DNA hybridsmain replicative polymeraseCatalyzes the carboxylation of acetyl-CoA to malonyl-CoAcatalyzes the conversion of a phosphate monoester to an alcohol and a phosphateCatalyzes the repair of proteins damaged by isoaspartyl formationBinds with the catalytic core of RNA polymerase to produce the holoenzymepreviously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)Identified by sequence similarity; similar to NC_007005:4533416..4533538, NC_005773:1684970..1685092identified by Glimmer2; putativeidentified by Glimmer2; putative

Page 51: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by match to PFAM protein family HMM PF01476similar to GP:4545127, and GP:4545127; identified by sequence similarity; putative

Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATPcatalyzes the formation of adenosylcob(III)yrinic acid a,c-diamide from cob(I)yrinic acid a,c-diamide

identified by match to PFAM protein family HMM PF03349

similar to GP:9946943; identified by sequence similarity; putativesimilar to GP:9947362; identified by sequence similarity; putative

negatively supercoils closed circular double-stranded DNACatalyzes the formation of (d)CDP from ATP and (d)CMP

putative metalloproteasecatalyzes the formation of oxalozcetate and L-glutamate from L-aspartate and 2-oxoglutaratesimilar to GB:M81934, SP:P30305, PID:1770370, and PID:180173; identified by sequence similarity; putativesimilar to SP:P95745; identified by sequence similarity; putativesimilar to SP:P15993; identified by sequence similarity; putativeRibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1 -D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP

identified by match to PFAM protein family HMM PF03313similar to GP:15076316, and GP:11990463; identified by sequence similarity; putativesimilar to SP:Q9LCC2, and GP:17980436; identified by sequence similarity; putativesimilar to GP:13183737, and SP:Q07510; identified by sequence similarity; putativecatalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxidesimilar to SP:P75935, GB:Z29327, and PID:441236; identified by sequence similarity; putativesimilar to SP:P75937; identified by sequence similarity; putativesimilar to SP:P75938; identified by sequence similarity; putativesimilar to SP:Q07510; identified by sequence similarity; putativesimilar to GP:3851066, and GP:3851064; identified by sequence similarity; putativesimilar to GP:2384651, GB:M32101, SP:P16701, PID:145659, GB:U00096, PID:1788764, PID:1799843, and PID:1799853; identified by sequence similarity; putativesimilar to GP:7081488, and SP:P24216; identified by sequence similarity; putativesimilar to SP:Q01960; identified by sequence similarity; putativedirects late flagellar gene expressionCatalyzes the conversion of citrate to isocitrateidentified by Glimmer2; putativeinvolved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymeridentified by match to TIGR protein family HMM TIGR01449identified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putative

catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphatesimilar to GP:154976, and SP:P07661; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF01227identified by Glimmer2; putative

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

Page 52: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Presumed to be involved in the biosynthesis of pyoverdine due to proximity to the rest of the pyoverdine biosynthetic gene cluster. Possibly acts to release the pyoverdine chromophore precursor from PvsA.; similar to GP:9948471; identified by sequence similarity; putativeCatalyzes the specific recognition and activation of amino acids during peptide synthesiscatalyzes the reversible formation of diaminobutyrate and 2-oxoglutarate from glutamate and L-aspartic beta-semialdehydesimilar to GP:15159638; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF01297

similar to SP:P31304; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF03929Present adjacent to pyoverdine biosynthetic genes; similar to GP:1890776; identified by sequence similarity; putativeThis synthetase is the second module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the third module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the fourth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; similar to GP:13094061; identified by sequence similarity; putativeThis synthetase is the fifth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore. This module terminates the peptide chain with a thioesterase domain at the C-terminus.; identified by match to PFAM protein family HMM PF02875similar to SP:P42512, GB:L17325, and PID:306323; identified by sequence similarity; putativesimilar to GP:466460, GB:X06325, SP:P09002, and PID:1333690; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03781similar to GP:13506638; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF02776identified by match to TIGR protein family HMM TIGR01730identified by match to PFAM protein family HMM PF01804

catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalatecatalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/Dcatalyzes the oxidation of 3-isopropylmalate to 3-carboxy-4-methyl-2-oxopentanoate in leucine biosynthesiscatalyzes the formation of aspartate semialdehyde from aspartyl phosphateidentified by match to PFAM protein family HMM PF02746similar to GP:15159729, and SP:P38974; identified by sequence similarity; putativesimilar to GP:11559420; identified by sequence similarity; putativesimilar to GP:9947544, and SP:P10446; identified by sequence similarity; putativesimilar to SP:P10445, GB:X62643, SP:P39479, and PID:46682; identified by sequence similarity; putativeConverts succinate to fumarate as part of the TCA cycle. It is the only membrane bound enzyme in the TCA cyclepart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane componentscatalyzes the interconversion of succinyl-CoA and succinatemolecular chaperonecatalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to 2,3-decenoyl-ACP or 3,4-decenoyl-ACP

catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphatecatalyzes the reduction of 3 -phosphoadenylyl sulfate into sulfitesimilar to GP:9947735; identified by sequence similarity; putativeDNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to SP:P22986, GB:J03827, SP:P16990, SP:P16991, PID:181486, PID:340419, and PID:454152; identified by sequence similarity; putativeInvolved in nucleic acid metabolismsimilar to SP:P00437, GB:M30496, SP:P15374, and PID:340074; identified by sequence similarity; putativesimilar to GP:10442739, and SP:P00436; identified by sequence similarity; putativeCatalyzes the cycloisomerization of cis,cis-muconatesimilar to GP:15141381; identified by sequence similarity; putative

identified by Glimmer2; putativeBinds to the 30S ribosomal subunit and enhances its availability for the initiation of protein synthesis

This protein binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunitcatalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium

Page 53: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by match to PFAM protein family HMM PF01966similar to SP:P18021, SP:P06615, GB:X04967, PID:144169, and PID:147038; identified by sequence similarity; putativeidentified by Glimmer2; putativecatalyzes the formation of isochorismate from chorismatecatalyzes the interconversion of chorismate to prephenateActivates salicylate by adenylation and transfers the salicylyl moiety to irp2, the non-ribosomal peptide synthetase component of yersiniabactin synthetase. Yersiniabactin is a siderophore.; similar to SP:P40871, GP:2765198, GB:X68560, SP:Q02447, PID:338303, and PID:38418; identified by sequence similarity; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis enzyme reduces the carbon-nitrogen bond of the second of three thiazoline rings of the siderophore yersiniabactin. Most probably this reduction takes place while an intermediate of the biosynthesis is still bound to irp2, the non-ribosomal peptide synthetase component, due to the presence of a conserved domain likely to function as a docking site for the reductase.; similar to GP:2765196; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon; similar to GP:11493181; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon.; similar to GP:11493180; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putative

previously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putativesimilar to GP:15140237, and SP:P25526; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF04020similar to GP:2293420; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF02782similar to SP:P39160; identified by sequence similarity; putative

similar to GP:2293414; identified by sequence similarity; putativesimilar to SP:P04042; identified by sequence similarity; putativeCatalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoAcan catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5 -phosphatesidentified by Glimmer2; putative

similar to SP:P37901, SP:P14250, and PID:148571; identified by sequence similarity; putative

identified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF02843This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to GP:9949964; identified by sequence similarity; putativesimilar to GB:U13737, GB:U13738, GB:U26943, SP:P42574, PID:561666, PID:561668, and PID:857569; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00034similar to GP:17427046; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF02630identified by Glimmer2; putativeidentified by match to TIGR protein family HMM TIGR01783identified by Glimmer2; putativepreviously known as HopPtoL (PMID 12032338; Petnicki-Ocwieja et al, 2002)similar to GP:12722244; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03781

similar to GP:13926036; identified by sequence similarity; putativeidentified by Glimmer2; putativealso known as AvrPtoB; similar to GP:5702216, and GP:18535643; identified by sequence similarity; putativesimilar to GP:9948480; identified by sequence similarity; putativesimilar to SP:P80239; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by match to TIGR protein family HMM TIGR00338

catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconate

Page 54: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

catalyzes the hydrolytic cleavage of the 4 -phosphopantetheine residue from ACP

identified by Glimmer2; putativesimilar to GP:15075777; identified by sequence similarity; putativesimilar to SP:Q52995; identified by sequence similarity; putativesimilar to SP:P45359; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF00512similar to SP:P06128; identified by sequence similarity; putativesimilar to SP:P32140, and SP:P32140; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR00034similar to GP:2981048, and SP:P00089; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01804identified by match to PFAM protein family HMM PF02974similar to SP:P06967; identified by sequence similarity; putativeidentified by Glimmer2; putative

Stimulates the activities of the other two initiation factors, IF-2 and IF-3

similar to GP:9948694, and GP:9948694; identified by sequence similarity; putativeCatalyzes the first step in the glyoxalate cycle, which converts lipids to carbohydratesCatalyzes the transfer of electrons from NADH to ubiquinoneThe point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen

Produces ATP from ADP in the presence of a proton gradient across the membrane. Rotates with gamma and delta subunits in a cylinder formed of alternating alpha and beta subunits

Catalyzes the transfer of electrons from NADH to ubiquinoneCatalyzes the transfer of electrons from NADH to ubiquinoneCatalyzes the transfer of electrons from NADH to ubiquinoneCatalyzes the transfer of electrons from NADH to ubiquinoneCatalyzes the transfer of electrons from NADH to ubiquinone

identified by Glimmer2; putativeidentified by match to TIGR protein family HMM TIGR00039

identified by match to TIGR protein family HMM TIGR01783similar to GP:9478255, and GP:17984964; identified by sequence similarity; putativesimilar to SP:P18274; identified by sequence similarity; putativesimilar to SP:P42418; identified by sequence similarity; putativesimilar to SP:P26935, GB:Z14978, GB:X82206, SP:P42024, SP:P42025, PID:28346, PID:563883, PID:563886, and PID:563888; identified by sequence similarity; putativesimilar to SP:P42415; identified by sequence similarity; putativesimilar to SP:P42413; identified by sequence similarity; putativeRepresses a number of genes involved in the response to DNA damagecatalyzes the ATP-dependent breakage of signle-stranded DNA followed by passage and rejoining, maintains net negative superhelicitysimilar to GP:15077078, and SP:P21177; identified by sequence similarity; putativesimilar to GB:S54005, GB:M20259, GB:M92381, SP:P13472, PID:339661, PID:339687, and PID:339697; identified by sequence similarity; putativesimilar to GP:5881935; identified by sequence similarity; putativesimilar to GP:17431596, and GP:17431596; identified by sequence similarity; putative

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanineidentified by match to PFAM protein family HMM PF00903identified by match to PFAM protein family HMM PF02798

Page 55: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by match to TIGR protein family HMM TIGR01783identified by match to PFAM protein family HMM PF00672identified by match to PFAM protein family HMM PF00672similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putativesimilar to GP:12514379; identified by sequence similarity; putativesimilar to GP:4062579; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF04261identified by match to PFAM protein family HMM PF04302identified by Glimmer2; putativeidentified by Glimmer2; putativeplays a role in assembling DnaB onto the primer template and interacts with the core polymerasesimilar to SP:P55533; identified by sequence similarity; putative

similar to SP:P03753, and SP:P03753; identified by sequence similarity; putativesimilar to SP:P25184; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01293

3 -5 exonuclease of DNA polymerase IIIAn endonuclease which specifically degrades the RNA of RNA-DNA hybridsidentified by Glimmer2; putative

similar to GP:5822345, and SP:P29132; identified by sequence similarity; putativeTig; RopA; peptidyl-prolyl cis/trans isomerase; promotes folding of newly synthesized proteins; binds ribosomal 50S subunit; forms a homodimersimilar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putativeCatalyzes the conversion of citrate to isocitrateidentified by match to PFAM protein family HMM PF02812identified by Glimmer2; putativesimilar to SP:P39293, and SP:P39293; identified by sequence similarity; putativesimilar to GP:12324950, and SP:P04825; identified by sequence similarity; putativeidentified by Glimmer2; putativeCatalyzes the carboxylation of acetyl-CoA to malonyl-CoA

Catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACPidentified by match to PFAM protein family HMM PF03454poorly understood protein involved in fatty acid and phospholipid biosynthesisidentified by Glimmer2; putativesimilar to GB:U07987, SP:P01871, PID:184726, and PID:468239; identified by sequence similarity; putativeBlocks the formation of polar Z-ring septumsidentified by match to PFAM protein family HMM PF01547identified by match to PFAM protein family HMM PF00903

identified by Glimmer2; putativesimilar to GP:3089521, and GP:3089521; identified by sequence similarity; putativecatalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesisidentified by match to PFAM protein family HMM PF00753identified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF005783 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphateforms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolAsimilar to GP:5514778, and SP:P50600; identified by sequence similarity; putativesimilar to SP:P50599, GB:U07988, SP:P01871, PID:184726, PID:468241, PID:499592, PID:567116, and PID:567175; identified by sequence similarity; putativesimilar to SP:P05828; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03061similar to SP:P37960; identified by sequence similarity; putativesimilar to SP:P80415; identified by sequence similarity; putativesimilar to SP:P32722, and SP:P32722; identified by sequence similarity; putative

Page 56: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:309853; identified by sequence similarity; putativesimilar to GP:8919960, and SP:P03034; identified by sequence similarity; putativesimilar to SP:P75802, SP:Q05426, and PID:150149; identified by sequence similarity; putativesimilar to SP:Q44532, and SP:Q44532; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01387catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAssimilar to GP:7243294, and SP:P00213; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03061previously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to SP:P04816, and SP:P21175; identified by sequence similarity; putative

similar to GP:13625473, and SP:P80415; identified by sequence similarity; putativeRequired for both initiation of translation and elongation of protein synthesisCatalyzes ATP + L-citrulline + L-aspartate = AMP + diphosphate + (N(omega)-L-arginino)succinatecatalyzes the formation of N-carbamoyl-L-aspartate from (S)-dihydroorotate in pyrimidine biosynthesisResponsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A)similar to GP:4378826, and SP:P13655; identified by sequence similarity; putativesimilar to SP:P22759, and SP:P22759; identified by sequence similarity; putativeConverts glycerol and ADP to glycerol-3-phosphate and ADPsimilar to SP:Q51391; identified by sequence similarity; putative

similar to SP:P15877; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00382identified by Glimmer2; putativesimilar to SP:P26844; identified by sequence similarity; putativesimilar to SP:P38108; identified by sequence similarity; putativesimilar to SP:P38107; identified by sequence similarity; putativeDNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to GP:11128402; identified by sequence similarity; putativesimilar to GP:11128403; identified by sequence similarity; putativesimilar to GP:11128404, and GP:11128404; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF01381identified by match to PFAM protein family HMM PF00583similar to SP:P06758; identified by sequence similarity; putativesimilar to SP:P33363, SP:P17447, GB:X52905, PID:48716, GB:U00096, PID:1657512, and PID:1786506; identified by sequence similarity; putativesimilar to GP:15159267; identified by sequence similarity; putative

similar to GP:17428837; identified by sequence similarity; putative

similar to GB:J05428, SP:P16662, GB:S82485, and PID:340080; identified by sequence similarity; putativesimilar to GP:7649485; identified by sequence similarity; putativeidentified by Glimmer2; putativepreviously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:12620626, and GP:12620626; identified by sequence similarity; putativesimilar to GP:7799213; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF00970similar to SP:P00923; identified by sequence similarity; putativesimilar to GP:3265044, and GP:16416915; identified by sequence similarity; putativesimilar to GP:15074498; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00724similar to SP:P53641; identified by sequence similarity; putative

Page 57: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P37147; identified by sequence similarity; putativeCatalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesissimilar to GP:9950620; identified by sequence similarity; putativesimilar to SP:P10408; identified by sequence similarity; putativeCatalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesisUDP-N-acetylglucosamine--N-acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; involved in cell wall formation; inner membrane-associated; last step of peptidoglycan synthesisUDP-N-acetylmuramoylalanine--D-glutamate ligase; involved in peptidoglycan biosynthesis; cytoplasmic; catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine during cell wall formationidentified by match to TIGR protein family HMM TIGR00252similar to SP:P25663, GB:S50157, GB:X60221, SP:P24539, and PID:509291; identified by sequence similarity; putativesimilar to GP:9864180, and SP:P05838; identified by sequence similarity; putativeL13 is associated with the antitermination complexcatalyzes a two-step reaction; first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNAin Rhizobium meliloti this protein is involved in the synthesis of nodulation factors that are active on the roots of alfalfa; catalyzes formation of activated sulfate intermediate; converts ATP and sulfate to diphosphate and adenylylsulfate and then ATP awith CysN catalyzes the formation of adenylylsulfate from sulfate and ATPadds enolpyruvyl to UDP-N-acetylglucosamine as a component of cell wall formationsimilar to GP:4336803; identified by sequence similarity; putativesimilar to GP:4336802; identified by sequence similarity; putativesimilar to GP:4336801, and GP:4336801; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF02470identified by match to TIGR protein family HMM TIGR00056identified by Glimmer2; putativesimilar to GB:M35657, SP:P15488, PID:145627, and PID:41161; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01186DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to GP:4138364, and GP:4138364; identified by sequence similarity; putativesimilar to GP:39453, SP:P28017, GB:X62377, and PID:39657; identified by sequence similarity; putativesimilar to GP:4581921, and GP:4704563; identified by sequence similarity; putativeclass II family; tetrameric enzyme; fumarase C; reversibly converts (S)-malate to fumarate and water; functions in the TCA cycleAllows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes

similar to GP:9951008; identified by sequence similarity; putativesimilar to SP:P33582; identified by sequence similarity; putativeReversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate

necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary compcatalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis

heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria

binds to ssrA RNA and is required for its sucessful binding to ribosomesidentified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF00141identified by match to PFAM protein family HMM PF00990similar to SP:P42240, and SP:P39829; identified by sequence similarity; putativesimilar to SP:P23847; identified by sequence similarity; putativesimilar to SP:P23847; identified by sequence similarity; putativesimilar to GP:9950741, and SP:P32722; identified by sequence similarity; putative

identified by Glimmer2; putative

Page 58: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

glycine betaine L-proline ABC transporter, periplasmic substrate-binding protein

Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2identified by Glimmer2; putativeidentified by Glimmer2; putativesimilar to GB:M59828, GB:M24744, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, PID:639910, GB:M59830, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, and PID:639910; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00764Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).identified by Glimmer2; putativePreviously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativesimilar to GP:15075123, and GP:13926142; identified by sequence similarity; putativesimilar to GP:15082090; identified by sequence similarity; putativesimilar to GB:X61072, and PID:33512; identified by sequence similarity; putativesimilar to SP:P25396, GB:S71240, GB:M99649, GB:Z12354, GB:X92288, PID:1228916, PID:1280224, PID:1402821, PID:1480263, PID:1791009, PID:2065185, PID:2145182, PID:2345010, PID:31006, PID:32931, PID:33581, PID:38341, PID:392758, PID:483382, PID:495993, PID:496014, PID:553446, PID:553453, PID:553456, PID:587247, PID:587251, PID:619627, PID:904790, PID:939890, PID:945217, PID:971198, PID:976299, PID:976304, PID:976315, and PID:976342; identified by sequence similarity; putative

identified by Glimmer2; putative

similar to GP:15157428; identified by sequence similarity; putativeProposed to be loaded with succinate semialdehyde as the starter unit for coronafacic acid biosynthesis. The ligase responsible for loading this ACP is probably the cfl gene immediately upstream. The succinate semialdehyde unit is proposed to be extended by one acetate unit, cyclized and dehydrated to yield CPC (cyclopentenone carboxylate) which is subsequently transferred to the polyketide synthetase, Cfa6.; similar to PIR:JC5745, SP:Q00767, GB:M76657, and PID:153292; identified by sequence similarity; putativeProbably involved in the final step of the biosynthesis of CPC (cyclopentenone carboxylate) on the acyl carrier protein Cfa1. Catalyzes the dehydration of the initial cyclization product.; similar to SP:P72238; identified by sequence similarity; putativePossibly involved in the biosynthesis of CPC (cyclopentenone carboxylate), an intermediate in the biosynthesis of coronafacic acid, from acetyl CoA and succinyl semialdehyde.; similar to PIR:JC5747, and GP:1655813; identified by sequence similarity; putativePossibly the ligase which activates coronafacic acid and transfers it to CoA or an acyl carrier protein.; similar to GP:7649554, and PIR:PC4426; identified by sequence similarity; putativeThis gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativeThe product of this reaction is butyryl-CoA which is required for the biosynthesis of coronafacic acid. In other organisms this activity is part of various pathways and is known as ccr, or ccrA.; similar to GP:4731329, and GP:15823984; identified by sequence similarity; putativeThis thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putativePreviously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918previously known as HopPtoAA (PMID 11872842; Guttman et al, 2002)

Probably acts to release coronamic acid from CmaA.; similar to GP:541616, GB:L22343, and PID:402148; identified by sequence similarity; putativeThis gene is found within the coronatine biosynthetic gene cluster and may have a function in that process.; similar to GP:3256494, GB:X05257, and PID:46457; identified by sequence similarity; putativesimilar to GP:541617; identified by sequence similarity; putativepreviously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987identified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativePreviously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:6472620; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to SP:P35076, GB:X64876, and PID:580818; identified by sequence similarity; putativeThe C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putativepreviously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putativesimilar to SP:P11886; identified by sequence similarity; putative

Catalyzes the radical-mediated insertion of two sulfur atoms into an acyl carrier protein (ACP) bound to an octanoyl group to produce a lipoyl group

identified by Glimmer2; putativeMethylates ribosomal protein L11

high affinity branched-chain amino acid ABC transporter, periplasmic amino acid-binding proteincatalyzes the formation of nictonate and 5-phospho-alpha-D-ribose 1-diphosphate from nicotinate D-ribonucleotide and diphosphate

Page 59: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

binds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21

Catalyzes the forst step in the biosynthesis of 2-methylthio-N6-(delta(2)-isopentyl)-adenosine adjacent to the anticodon of several tRNA speciesCatalyzes the decarboxylation of phosphatidyl-L-serine to phosphatidylethanoleaminesimilar to GP:9951239; identified by sequence similarity; putativedecatenates newly replicated chromosomal DNA and relaxes positive and negative DNA supercoiling

similar to SP:P24562, and SP:P24562; identified by sequence similarity; putative

catalyzes the formation of O-acetyl-L-homoserine from homoserine and acetyl-CoA in methionine biosynthesisidentified by match to PFAM protein family HMM PF04264similar to SP:P75925; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01110identified by match to PFAM protein family HMM PF02374

heat shock protein involved indegradation of misfolded proteinsheat shock protein involved in degradation of misfolded proteinssimilar to GP:17402510, and GP:17402510; identified by sequence similarity; putative

catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribolsyl)-ATP in histidine biosynthesisidentified by Glimmer2; putativesimilar to GP:15155399; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF03573

similar to GP:15980232, and GP:15980232; identified by sequence similarity; putativeCatalyzes the conversion of 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]- 1-(5-phosphoribosyl)imidazole-4-carboxamide and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide and glutamateidentified by match to PFAM protein family HMM PF02987similar to GP:8037768, and GP:8037768; identified by sequence similarity; putativepreviously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to GP:12544544, and GP:15159386; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03746identified by Glimmer2; putativesimilar to GP:2290992; identified by sequence similarity; putativesimilar to GB:X74143, SP:P55316, PID:516383, and PID:967048; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF00908identified by match to TIGR protein family HMM TIGR00052similar to GP:15156635; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00498identified by Glimmer2; putativeidentified by Glimmer2; putative

Page 60: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:7295702; identified by sequence similarity; putativesimilar to GP:14524293; identified by sequence similarity; putativeidentified by Glimmer2; putative

identified by match to TIGR protein family HMM TIGR00838identified by match to PFAM protein family HMM PF03239

Converts oxaloacetate to phosphoenolpyruvate using ATP as an energy sourceCatalyzes the formation of malnoyl-CoA, which in turn controls the rate of fatty acid metabolismidentified by Glimmer2; putative

identified by Glimmer2; putativeidentified by match to TIGR protein family HMM TIGR01250Produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is a regulatory subunit

protein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substratessimilar to GP:8572766; identified by sequence similarity; putativesimilar to GP:15667830, and GP:15667830; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03132identified by match to PFAM protein family HMM PF01839identified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putativesimilar to SP:P05839, and SP:P05839; identified by sequence similarity; putativesimilar to GP:14488264; identified by sequence similarity; putativesimilar to GP:6273613; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00991This gene assignment is based in part on its location adjacent to a Tn3 family transposase.; similar to SP:P30739; identified by sequence similarity; putativeAlso known as AvrPphE; similar to GP:571514; identified by sequence similarity; putativeidentified by Glimmer2; putativePreviously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putativesimilar to GP:17431229, and GP:17982579; identified by sequence similarity; putativesimilar to GP:13926144, and GP:13926145; identified by sequence similarity; putative

Page 61: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

previously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putativePreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putative

similar to GB:L19158, GB:D26443, GB:U03504, GB:Z31713, SP:P43003, PID:487339, PID:607113, PID:825504, and PID:825663; identified by sequence similarity; putative

similar to SP:P23883, GB:M11147, GB:M10119, GB:M12938, GB:X03742, GB:X03743, SP:P02792, PID:1340145, PID:1340146, PID:182514, PID:182516, PID:182518, PID:2230869, and PID:28519; identified by sequence similarity; putative

similar to SP:P23929, GB:M16447, GB:X04882, SP:P09417, PID:181553, and PID:30819; identified by sequence similarity; putative

PEP carboxykinase; PEP carboxylase; PEPCK; catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using ATP

similar to SP:P06997, GB:M25322, GB:M60218, GB:M60219, GB:M60222, GB:M60223, GB:M60224, GB:M60225, GB:M60226, GB:M60227, GB:M60228, GB:M60229, GB:M60230, GB:M60231, GB:M60232, GB:M60233, GB:M60234, GB:M60235, SP:P16109, PID:183389, and PID:183391; identified by sequence similarity; putative

catalyzes the formation of dihydrolipoylprotein from S-aminomethyldihydrolipoprotein in the glycine cleavage system

similar to SP:Q46851, GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

: Differentially regulated genes identified at a p value less than or equal to 0.05 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log 2.

Page 62: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P22539, GB:M60111, GB:X59593, PID:147848, PID:396397, PID:42975, GB:U00096, and PID:1790497; identified by sequence similarity; putative

similar to SP:P46154, GB:X64318, GB:U26173, GB:S79880, PID:1237118, and PID:30956; identified by sequence similarity; putative

Catalyzes the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases in 16S rRNA

previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586Catalyzes the conversion of 1-(2-carboxyphenylamino)1-deoxy-D-ribulose 5 phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate during the biopsynthesis of tryptophan

catalyzes the reduction of N-acetyl-5-glutamyl phosohate to N-acetyl-glutamate 5-semialdehyde in arginine biosynthesis

present in two forms; L12 is normal, while L7 is aminoacylated at the N-terminal serine; the only multicopy ribosomal protein; 4:1 ratio of L7/L12 per ribosome; two L12 dimers bind L10; critically important for translation efficiency and fidelity; stimulatImportant for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S sOne of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center

Binds specifically to 23S rRNA during the early stages of 50S assembly. It makes multiple contacts with different domains of te 23S rRNA in the assembled 50S subunit and ribosomeforms a complex with S10 and S14; binds the lower part of the 30S subunit head and the mRNA in the complete ribosome to position it for translation

Mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance

located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosome

Page 63: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

Also known as ORF24 (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to TIGR protein family HMM TIGR01449

previously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putativeIdentified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

similar to GP:5919222, GB:M13699, GB:D00025, GB:X69706, GB:M13536, GB:X04136, GB:X04137, GB:X04138, SP:P00450, PID:1335036, PID:1335037, PID:1666064, and PID:180249; identified by sequence similarity; putative

Also known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

similar to GP:4837634, GB:J02958, GB:M35074, GB:X54559, GB:U11813, GB:M35073, SP:P08581, PID:307196, PID:386868, PID:487742, PID:530800, and PID:625086; identified by sequence similarity; putative

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

Page 64: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:3142220, GB:X04409, GB:X56009, GB:M21139, GB:M21740, GB:M21140, GB:M21741, GB:M21141, GB:M21142, GB:X04408, GB:X07036, GB:M14631, GB:U12466, SP:P04895, PID:31913, PID:386745, PID:386746, and PID:527671; identified by sequence similarity; putative

involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymersimilar to GB:M60091, GB:L46359, GB:L46360, GB:L46361, GB:L46362, GB:L48713, GB:L48715, GB:L48716, SP:P07902, PID:1066737, PID:1066749, PID:1066751, PID:1066753, PID:182951, PID:306759, PID:950351, PID:950353, PID:950355, PID:950357, PID:950365, PID:950367, PID:950369, PID:950377, PID:950381, PID:950383, PID:950391, PID:950393, PID:950395, PID:950397, PID:950399, PID:950401, PID:950403, and PID:950405; identified by sequence similarity; putative

catalyzes the formation of pyruvate and glyoxylate from 4-hydroxy-2-oxoglutarate; or pyruvate and D-glyceraldehyde 3-phosphate from 2-dehydro-3-deoxy-D-glyconate 6-phosphate

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

Page 65: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putative

Also known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

member of preprotein translocase; forms a heterotrimer with SecD and SecF; links the SecD/SecF/YajC/YidC complex with the SecY/SecE/SecG complex

adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesisin Pseudomonas aeruginosa this enzyme is a trimer of dimers; essential for membrane formation; performs third step of type II fatty acid biosynthesis; catalyzes dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP

catalyzes the formation of lipid A disaccharide from UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate; lipid A disaccharide is a precursor of lipid A that anchors LPS to the OM

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)

Page 66: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP

RibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1 -D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-

similar to GP:2384651, GB:M32101, SP:P16701, PID:145659, GB:U00096, PID:1788764, PID:1799843, and PID:1799853; identified by sequence similarity; putative

involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymer

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

Page 67: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Presumed to be involved in the biosynthesis of pyoverdine due to proximity to the rest of the pyoverdine biosynthetic gene cluster. Possibly acts to release the pyoverdine chromophore precursor from PvsA.; similar to GP:9948471; identified by sequence similarity; putative

catalyzes the reversible formation of diaminobutyrate and 2-oxoglutarate from glutamate and L-aspartic beta-semialdehyde

Present adjacent to pyoverdine biosynthetic genes; similar to GP:1890776; identified by sequence similarity; putativeThis synthetase is the second module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the third module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the fourth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; similar to GP:13094061; identified by sequence similarity; putativeThis synthetase is the fifth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore. This module terminates the peptide chain with a thioesterase domain at the C-terminus.; identified by match to PFAM protein family HMM PF02875

catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/D

part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components

catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to SP:P22986, GB:J03827, SP:P16990, SP:P16991, PID:181486, PID:340419, and PID:454152; identified by sequence similarity; putative

This protein binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunitcatalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium

Page 68: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P18021, SP:P06615, GB:X04967, PID:144169, and PID:147038; identified by sequence similarity; putative

Activates salicylate by adenylation and transfers the salicylyl moiety to irp2, the non-ribosomal peptide synthetase component of yersiniabactin synthetase. Yersiniabactin is a siderophore.; similar to SP:P40871, GP:2765198, GB:X68560, SP:Q02447, PID:338303, and PID:38418; identified by sequence similarity; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis enzyme reduces the carbon-nitrogen bond of the second of three thiazoline rings of the siderophore yersiniabactin. Most probably this reduction takes place while an intermediate of the biosynthesis is still bound to irp2, the non-ribosomal peptide synthetase component, due to the presence of a conserved domain likely to function as a docking site for the reductase.; similar to GP:2765196; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon; similar to GP:11493181; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon.; similar to GP:11493180; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putative

previously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putative

can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5 -phosphates

This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putative

similar to GB:U13737, GB:U13738, GB:U26943, SP:P42574, PID:561666, PID:561668, and PID:857569; identified by sequence similarity; putative

Page 69: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

The point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen

Produces ATP from ADP in the presence of a proton gradient across the membrane. Rotates with gamma and delta subunits in a cylinder formed of alternating alpha and beta subunits

similar to SP:P26935, GB:Z14978, GB:X82206, SP:P42024, SP:P42025, PID:28346, PID:563883, PID:563886, and PID:563888; identified by sequence similarity; putative

catalyzes the ATP-dependent breakage of signle-stranded DNA followed by passage and rejoining, maintains net negative superhelicity

similar to GB:S54005, GB:M20259, GB:M92381, SP:P13472, PID:339661, PID:339687, and PID:339697; identified by sequence similarity; putative

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine

Page 70: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

Tig; RopA; peptidyl-prolyl cis/trans isomerase; promotes folding of newly synthesized proteins; binds ribosomal 50S subunit; forms a homodimersimilar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP

catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis

3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphateforms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolA

similar to SP:P50599, GB:U07988, SP:P01871, PID:184726, PID:468241, PID:499592, PID:567116, and PID:567175; identified by sequence similarity; putative

Page 71: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs

previously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putative

Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A)

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

similar to SP:P33363, SP:P17447, GB:X52905, PID:48716, GB:U00096, PID:1657512, and PID:1786506; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).

Page 72: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesisUDP-N-acetylglucosamine--N-acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; involved in cell wall formation; inner membrane-associated; last step of peptidoglycan synthesisUDP-N-acetylmuramoylalanine--D-glutamate ligase; involved in peptidoglycan biosynthesis; cytoplasmic; catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine during cell wall formation

similar to SP:P25663, GB:S50157, GB:X60221, SP:P24539, and PID:509291; identified by sequence similarity; putative

catalyzes a two-step reaction; first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNAin Rhizobium meliloti this protein is involved in the synthesis of nodulation factors that are active on the roots of alfalfa; catalyzes formation of activated sulfate intermediate; converts ATP and sulfate to diphosphate and adenylylsulfate and then ATP a

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

class II family; tetrameric enzyme; fumarase C; reversibly converts (S)-malate to fumarate and water; functions in the TCA cycleAllows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes

Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate

necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary compcatalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis

heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria

Page 73: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:M59828, GB:M24744, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, PID:639910, GB:M59830, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, and PID:639910; identified by sequence similarity; putative

Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

similar to SP:P25396, GB:S71240, GB:M99649, GB:Z12354, GB:X92288, PID:1228916, PID:1280224, PID:1402821, PID:1480263, PID:1791009, PID:2065185, PID:2145182, PID:2345010, PID:31006, PID:32931, PID:33581, PID:38341, PID:392758, PID:483382, PID:495993, PID:496014, PID:553446, PID:553453, PID:553456, PID:587247, PID:587251, PID:619627, PID:904790, PID:939890, PID:945217, PID:971198, PID:976299, PID:976304, PID:976315, and PID:976342; identified by sequence similarity; putative

Proposed to be loaded with succinate semialdehyde as the starter unit for coronafacic acid biosynthesis. The ligase responsible for loading this ACP is probably the cfl gene immediately upstream. The succinate semialdehyde unit is proposed to be extended by one acetate unit, cyclized and dehydrated to yield CPC (cyclopentenone carboxylate) which is subsequently transferred to the polyketide synthetase, Cfa6.; similar to PIR:JC5745, SP:Q00767, GB:M76657, and PID:153292; identified by sequence similarity; putativeProbably involved in the final step of the biosynthesis of CPC (cyclopentenone carboxylate) on the acyl carrier protein Cfa1. Catalyzes the dehydration of the initial cyclization product.; similar to SP:P72238; identified by sequence similarity; putativePossibly involved in the biosynthesis of CPC (cyclopentenone carboxylate), an intermediate in the biosynthesis of coronafacic acid, from acetyl CoA and succinyl semialdehyde.; similar to PIR:JC5747, and GP:1655813; identified by sequence similarity; putativePossibly the ligase which activates coronafacic acid and transfers it to CoA or an acyl carrier protein.; similar to GP:7649554, and PIR:PC4426; identified by sequence similarity; putativeThis gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativeThe product of this reaction is butyryl-CoA which is required for the biosynthesis of coronafacic acid. In other organisms this activity is part of various pathways and is known as ccr, or ccrA.; similar to GP:4731329, and GP:15823984; identified by sequence similarity; putativeThis thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putativePreviously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918

Probably acts to release coronamic acid from CmaA.; similar to GP:541616, GB:L22343, and PID:402148; identified by sequence similarity; putativeThis gene is found within the coronatine biosynthetic gene cluster and may have a function in that process.; similar to GP:3256494, GB:X05257, and PID:46457; identified by sequence similarity; putative

previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987

Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).

The C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putativepreviously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putative

Catalyzes the radical-mediated insertion of two sulfur atoms into an acyl carrier protein (ACP) bound to an octanoyl group to produce a lipoyl group

catalyzes the formation of nictonate and 5-phospho-alpha-D-ribose 1-diphosphate from nicotinate D-ribonucleotide and diphosphate

Page 74: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the forst step in the biosynthesis of 2-methylthio-N6-(delta(2)-isopentyl)-adenosine adjacent to the anticodon of several tRNA species

Catalyzes the conversion of 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]- 1-(5-phosphoribosyl)imidazole-4-carboxamide and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide and glutamate

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

Page 75: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is a regulatory subunit

protein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substrates

This gene assignment is based in part on its location adjacent to a Tn3 family transposase.; similar to SP:P30739; identified by sequence similarity; putative

Previously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 76: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P23883, GB:M11147, GB:M10119, GB:M12938, GB:X03742, GB:X03743, SP:P02792, PID:1340145, PID:1340146, PID:182514, PID:182516, PID:182518, PID:2230869, and PID:28519; identified by sequence similarity; putative

similar to SP:P06997, GB:M25322, GB:M60218, GB:M60219, GB:M60222, GB:M60223, GB:M60224, GB:M60225, GB:M60226, GB:M60227, GB:M60228, GB:M60229, GB:M60230, GB:M60231, GB:M60232, GB:M60233, GB:M60234, GB:M60235, SP:P16109, PID:183389, and PID:183391; identified by sequence similarity; putative

Page 77: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

present in two forms; L12 is normal, while L7 is aminoacylated at the N-terminal serine; the only multicopy ribosomal protein; 4:1 ratio of L7/L12 per ribosome; two L12 dimers bind L10; critically important for translation efficiency and fidelity; stimulatImportant for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s

Page 78: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

Identified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

similar to GP:5919222, GB:M13699, GB:D00025, GB:X69706, GB:M13536, GB:X04136, GB:X04137, GB:X04138, SP:P00450, PID:1335036, PID:1335037, PID:1666064, and PID:180249; identified by sequence similarity; putative

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

Page 79: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:3142220, GB:X04409, GB:X56009, GB:M21139, GB:M21740, GB:M21140, GB:M21741, GB:M21141, GB:M21142, GB:X04408, GB:X07036, GB:M14631, GB:U12466, SP:P04895, PID:31913, PID:386745, PID:386746, and PID:527671; identified by sequence similarity; putative

involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymersimilar to GB:M60091, GB:L46359, GB:L46360, GB:L46361, GB:L46362, GB:L48713, GB:L48715, GB:L48716, SP:P07902, PID:1066737, PID:1066749, PID:1066751, PID:1066753, PID:182951, PID:306759, PID:950351, PID:950353, PID:950355, PID:950357, PID:950365, PID:950367, PID:950369, PID:950377, PID:950381, PID:950383, PID:950391, PID:950393, PID:950395, PID:950397, PID:950399, PID:950401, PID:950403, and PID:950405; identified by sequence similarity; putative

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 80: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putative

Page 81: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP

RibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1 -D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-

involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymer

Page 82: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Presumed to be involved in the biosynthesis of pyoverdine due to proximity to the rest of the pyoverdine biosynthetic gene cluster. Possibly acts to release the pyoverdine chromophore precursor from PvsA.; similar to GP:9948471; identified by sequence similarity; putative

This synthetase is the second module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the third module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734This synthetase is the fourth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; similar to GP:13094061; identified by sequence similarity; putativeThis synthetase is the fifth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore. This module terminates the peptide chain with a thioesterase domain at the C-terminus.; identified by match to PFAM protein family HMM PF02875

part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components

catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium

Page 83: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Activates salicylate by adenylation and transfers the salicylyl moiety to irp2, the non-ribosomal peptide synthetase component of yersiniabactin synthetase. Yersiniabactin is a siderophore.; similar to SP:P40871, GP:2765198, GB:X68560, SP:Q02447, PID:338303, and PID:38418; identified by sequence similarity; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis enzyme reduces the carbon-nitrogen bond of the second of three thiazoline rings of the siderophore yersiniabactin. Most probably this reduction takes place while an intermediate of the biosynthesis is still bound to irp2, the non-ribosomal peptide synthetase component, due to the presence of a conserved domain likely to function as a docking site for the reductase.; similar to GP:2765196; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5 -phosphates

This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putative

Page 84: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

similar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Page 85: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

UDP-N-acetylglucosamine--N-acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; involved in cell wall formation; inner membrane-associated; last step of peptidoglycan synthesisUDP-N-acetylmuramoylalanine--D-glutamate ligase; involved in peptidoglycan biosynthesis; cytoplasmic; catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine during cell wall formation

in Rhizobium meliloti this protein is involved in the synthesis of nodulation factors that are active on the roots of alfalfa; catalyzes formation of activated sulfate intermediate; converts ATP and sulfate to diphosphate and adenylylsulfate and then ATP a

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes

necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary comp

Page 86: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:M59828, GB:M24744, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, PID:639910, GB:M59830, SP:P08107, PID:188488, PID:188490, PID:188528, PID:188530, PID:32483, PID:386785, and PID:639910; identified by sequence similarity; putative

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

similar to SP:P25396, GB:S71240, GB:M99649, GB:Z12354, GB:X92288, PID:1228916, PID:1280224, PID:1402821, PID:1480263, PID:1791009, PID:2065185, PID:2145182, PID:2345010, PID:31006, PID:32931, PID:33581, PID:38341, PID:392758, PID:483382, PID:495993, PID:496014, PID:553446, PID:553453, PID:553456, PID:587247, PID:587251, PID:619627, PID:904790, PID:939890, PID:945217, PID:971198, PID:976299, PID:976304, PID:976315, and PID:976342; identified by sequence similarity; putative

Proposed to be loaded with succinate semialdehyde as the starter unit for coronafacic acid biosynthesis. The ligase responsible for loading this ACP is probably the cfl gene immediately upstream. The succinate semialdehyde unit is proposed to be extended by one acetate unit, cyclized and dehydrated to yield CPC (cyclopentenone carboxylate) which is subsequently transferred to the polyketide synthetase, Cfa6.; similar to PIR:JC5745, SP:Q00767, GB:M76657, and PID:153292; identified by sequence similarity; putativeProbably involved in the final step of the biosynthesis of CPC (cyclopentenone carboxylate) on the acyl carrier protein Cfa1. Catalyzes the dehydration of the initial cyclization product.; similar to SP:P72238; identified by sequence similarity; putativePossibly involved in the biosynthesis of CPC (cyclopentenone carboxylate), an intermediate in the biosynthesis of coronafacic acid, from acetyl CoA and succinyl semialdehyde.; similar to PIR:JC5747, and GP:1655813; identified by sequence similarity; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativeThe product of this reaction is butyryl-CoA which is required for the biosynthesis of coronafacic acid. In other organisms this activity is part of various pathways and is known as ccr, or ccrA.; similar to GP:4731329, and GP:15823984; identified by sequence similarity; putativeThis thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putative

Page 87: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the conversion of 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]- 1-(5-phosphoribosyl)imidazole-4-carboxamide and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide and glutamate

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

Page 88: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 89: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P06997, GB:M25322, GB:M60218, GB:M60219, GB:M60222, GB:M60223, GB:M60224, GB:M60225, GB:M60226, GB:M60227, GB:M60228, GB:M60229, GB:M60230, GB:M60231, GB:M60232, GB:M60233, GB:M60234, GB:M60235, SP:P16109, PID:183389, and PID:183391; identified by sequence similarity; putative

Page 90: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

Page 91: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:M60091, GB:L46359, GB:L46360, GB:L46361, GB:L46362, GB:L48713, GB:L48715, GB:L48716, SP:P07902, PID:1066737, PID:1066749, PID:1066751, PID:1066753, PID:182951, PID:306759, PID:950351, PID:950353, PID:950355, PID:950357, PID:950365, PID:950367, PID:950369, PID:950377, PID:950381, PID:950383, PID:950391, PID:950393, PID:950395, PID:950397, PID:950399, PID:950401, PID:950403, and PID:950405; identified by sequence similarity; putative

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 92: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This synthetase is the fifth module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore. This module terminates the peptide chain with a thioesterase domain at the C-terminus.; identified by match to PFAM protein family HMM PF02875

Page 93: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This enzyme reduces the carbon-nitrogen bond of the second of three thiazoline rings of the siderophore yersiniabactin. Most probably this reduction takes place while an intermediate of the biosynthesis is still bound to irp2, the non-ribosomal peptide synthetase component, due to the presence of a conserved domain likely to function as a docking site for the reductase.; similar to GP:2765196; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putative

Page 94: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

similar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Page 95: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P25396, GB:S71240, GB:M99649, GB:Z12354, GB:X92288, PID:1228916, PID:1280224, PID:1402821, PID:1480263, PID:1791009, PID:2065185, PID:2145182, PID:2345010, PID:31006, PID:32931, PID:33581, PID:38341, PID:392758, PID:483382, PID:495993, PID:496014, PID:553446, PID:553453, PID:553456, PID:587247, PID:587251, PID:619627, PID:904790, PID:939890, PID:945217, PID:971198, PID:976299, PID:976304, PID:976315, and PID:976342; identified by sequence similarity; putative

Proposed to be loaded with succinate semialdehyde as the starter unit for coronafacic acid biosynthesis. The ligase responsible for loading this ACP is probably the cfl gene immediately upstream. The succinate semialdehyde unit is proposed to be extended by one acetate unit, cyclized and dehydrated to yield CPC (cyclopentenone carboxylate) which is subsequently transferred to the polyketide synthetase, Cfa6.; similar to PIR:JC5745, SP:Q00767, GB:M76657, and PID:153292; identified by sequence similarity; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

This thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putative

Page 96: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:M60091, GB:L46359, GB:L46360, GB:L46361, GB:L46362, GB:L48713, GB:L48715, GB:L48716, SP:P07902, PID:1066737, PID:1066749, PID:1066751, PID:1066753, PID:182951, PID:306759, PID:950351, PID:950353, PID:950355, PID:950357, PID:950365, PID:950367, PID:950369, PID:950377, PID:950381, PID:950383, PID:950391, PID:950393, PID:950395, PID:950397, PID:950399, PID:950401, PID:950403, and PID:950405; identified by sequence similarity; putative

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 97: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This enzyme reduces the carbon-nitrogen bond of the second of three thiazoline rings of the siderophore yersiniabactin. Most probably this reduction takes place while an intermediate of the biosynthesis is still bound to irp2, the non-ribosomal peptide synthetase component, due to the presence of a conserved domain likely to function as a docking site for the reductase.; similar to GP:2765196; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putative

Page 98: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P25396, GB:S71240, GB:M99649, GB:Z12354, GB:X92288, PID:1228916, PID:1280224, PID:1402821, PID:1480263, PID:1791009, PID:2065185, PID:2145182, PID:2345010, PID:31006, PID:32931, PID:33581, PID:38341, PID:392758, PID:483382, PID:495993, PID:496014, PID:553446, PID:553453, PID:553456, PID:587247, PID:587251, PID:619627, PID:904790, PID:939890, PID:945217, PID:971198, PID:976299, PID:976304, PID:976315, and PID:976342; identified by sequence similarity; putative

Proposed to be loaded with succinate semialdehyde as the starter unit for coronafacic acid biosynthesis. The ligase responsible for loading this ACP is probably the cfl gene immediately upstream. The succinate semialdehyde unit is proposed to be extended by one acetate unit, cyclized and dehydrated to yield CPC (cyclopentenone carboxylate) which is subsequently transferred to the polyketide synthetase, Cfa6.; similar to PIR:JC5745, SP:Q00767, GB:M76657, and PID:153292; identified by sequence similarity; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

Page 99: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 100: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

This gene consists of three complete condensation, adenylation, thiolation domain modules. The adenylation domains are specific for leucine, leucine and an unidentified amino acid. This NRPS lacks domains typical of the initiating or terminating components of NRPSs. The following gene which contains a terminal thioesterase domain is most likely its partner. There are no upstream genes which could function as the initiating domain. If expressed, these two genes would appear to generate and previously undescribed natural product.; similar to GP:3510629; identified by sequence similarity; putative

Page 101: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 102: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 103: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

locus_tag Regulatory Motif replicon a/b- a/c- a/b+ a/c+PSPTO_0003 RpoD NC_004578.1 NA 0.8431209 NA 0.6536205PSPTO_0022 NC_004578.1 NA NA NA -0.935258PSPTO_0044 HrpL NC_004578.1 NA NA -1.104889 -1.25709PSPTO_0061 HrpL NC_004578.1 NA NA NA -1.564984PSPTO_0062 NC_004578.1 -5.932367 NA -6.215231 NAPSPTO_0067 NC_004578.1 NA NA 3.8413599 3.909999PSPTO_0068 NC_004578.1 NA NA 4.6545684 4.6928295PSPTO_0069 NC_004578.1 NA NA 7.1372996 6.9590005PSPTO_0087 NC_004578.1 NA NA NA NAPSPTO_0152 NC_004578.1 NA NA NA NAPSPTO_0154 NC_004578.1 NA NA NA NAPSPTO_0156 NC_004578.1 NA NA NA 0.7385076PSPTO_0165 NC_004578.1 NA NA NA NAPSPTO_0206 NC_004578.1 NA NA NA -0.698857PSPTO_0211 NC_004578.1 NA NA NA 0.9724669PSPTO_0217 NC_004578.1 NA NA NA NAPSPTO_0219 NC_004578.1 NA NA NA 0.8202102PSPTO_0220 NC_004578.1 NA 0.6441649 NA 0.7811363PSPTO_0231 NC_004578.1 NA NA NA -0.807538PSPTO_0283 NC_004578.1 NA 3.7569243 NA 2.3385575PSPTO_0307 NC_004578.1 NA NA NA 2.6444655PSPTO_0309 NC_004578.1 NA NA NA 1.2623372PSPTO_0314 Fur NC_004578.1 NA NA 3.8027727 2.4570779PSPTO_0328 NC_004578.1 NA NA NA -0.848594PSPTO_0330 NC_004578.1 -1.430511 NA -1.537885 NAPSPTO_0351 NC_004578.1 NA NA NA NAPSPTO_0371 HrpL NC_004578.1 NA NA NA -0.733964PSPTO_0426 NC_004578.1 NA NA 1.0670061 0.859924PSPTO_0499 NC_004578.1 NA NA NA NAPSPTO_0503 HrpL NC_004578.1 NA NA -1.102675 -1.814398PSPTO_0524 HrpL NC_004578.1 NA NA -1.913905 -1.691704PSPTO_0539 NC_004578.1 NA NA NA 0.3819594PSPTO_0545 NC_004578.1 NA NA NA -1.966044PSPTO_0546 NC_004578.1 NA NA NA -1.156065PSPTO_0547 NC_004578.1 NA NA NA -0.889579PSPTO_0549 RpoD NC_004578.1 NA 0.5388626 NA 0.7144517PSPTO_0552 RpoD NC_004578.1 NA NA NA 0.654005PSPTO_0569 NC_004578.1 NA NA NA -1.397638PSPTO_0570 NC_004578.1 NA -1.328624 NA -1.46596PSPTO_0588 HrpL NC_004578.1 NA NA -0.583547 -1.015811PSPTO_0589 HrpL NC_004578.1 NA NA NA -1.19607PSPTO_0594 NC_004578.1 NA NA NA -0.412115PSPTO_0598 RpoD NC_004578.1 NA NA NA NAPSPTO_0603 NC_004578.1 NA NA NA NAPSPTO_0615 RpoD NC_004578.1 NA NA NA 0.2556747PSPTO_0621 RpoD NC_004578.1 NA NA NA 0.2456952PSPTO_0628 PvdS, RpoD NC_004578.1 NA NA NA 0.1819499PSPTO_0637 RpoD NC_004578.1 NA NA NA 0.1688892PSPTO_0638 RpoD NC_004578.1 NA NA NA 0.1649339PSPTO_0642 RpoD NC_004578.1 NA NA NA 0.174371PSPTO_0647 RpoD NC_004578.1 NA NA NA 0.2158567PSPTO_0648 RpoD NC_004578.1 NA NA NA 0.2412944PSPTO_0649 RpoD NC_004578.1 NA NA NA 0.208953PSPTO_0651 RpoD NC_004578.1 NA NA NA 0.234987PSPTO_0653 NC_004578.1 NA NA -3.539556 -3.450337PSPTO_0677 NC_004578.1 NA NA NA 0.6929601

Supplemental Table 2: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 104: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_0679 NC_004578.1 NA NA NA -2.302015PSPTO_0703 NC_004578.1 NA NA NA -0.651079PSPTO_0727 NC_004578.1 NA NA NA -0.598146PSPTO_0728 NC_004578.1 NA NA NA -0.603822PSPTO_0763 NC_004578.1 NA NA NA 0.5935469PSPTO_0776 NC_004578.1 NA NA NA -1.135762PSPTO_0806 RpoD NC_004578.1 NA NA NA NAPSPTO_0834 HrpL NC_004578.1 NA NA -1.093207 -0.858011PSPTO_0835 HrpL NC_004578.1 NA NA -0.837071 -0.827544PSPTO_0836 HrpL NC_004578.1 NA NA -1.783098 -1.505228PSPTO_0837 HrpL NC_004578.1 NA NA -1.232273 -1.066794PSPTO_0838 HrpL NC_004578.1 NA NA -1.249085 -1.297307PSPTO_0851 NC_004578.1 NA NA NA -1.783988PSPTO_0852 HrpL NC_004578.1 NA NA -1.244964 -2.186135PSPTO_0853 NC_004578.1 NA NA NA -0.813887PSPTO_0855 NC_004578.1 NA NA NA -1.191462PSPTO_0873 NC_004578.1 NA NA NA -0.685354PSPTO_0874 NC_004578.1 NA NA -1.005962 -1.270933PSPTO_0875 NC_004578.1 NA NA -2.219572 -2.925747PSPTO_0876 HrpL NC_004578.1 NA NA -0.643295 -1.101544PSPTO_0877 HrpL NC_004578.1 NA NA -0.989708 -1.954385PSPTO_0883 HrpL NC_004578.1 NA NA NA -1.916402PSPTO_0912 NC_004578.1 NA -2.000891 NA NAPSPTO_0927 NC_004578.1 NA NA NA NAPSPTO_0940 NC_004578.1 NA NA NA -0.406008PSPTO_0944 NC_004578.1 NA NA NA -0.294466PSPTO_0954 NC_004578.1 NA NA NA -0.701972PSPTO_0955 NC_004578.1 NA NA NA -1.053288PSPTO_0959 NC_004578.1 NA NA NA -0.354038PSPTO_0961 NC_004578.1 NA NA NA NAPSPTO_0994 NC_004578.1 NA NA NA -0.5896PSPTO_1102 NC_004578.1 NA 1.0986236 NA NAPSPTO_1134 NC_004578.1 NA NA NA 1.2205394PSPTO_1148 NC_004578.1 NA NA NA NAPSPTO_1164 NC_004578.1 NA NA -0.593324 NAPSPTO_1213 NC_004578.1 NA NA NA -0.615016PSPTO_1214 NC_004578.1 NA -2.95335 NA -2.559413PSPTO_1287 NC_004578.1 NA -0.480772 NA -0.34375PSPTO_1288 NC_004578.1 NA NA NA -1.508038PSPTO_1289 NC_004578.1 NA NA NA -1.020779PSPTO_1290 NC_004578.1 NA NA NA -0.442841PSPTO_1296 NC_004578.1 NA NA NA -0.565699PSPTO_1300 NC_004578.1 NA NA NA -0.357844PSPTO_1301 NC_004578.1 NA NA NA -0.457383PSPTO_1302 NC_004578.1 NA NA NA -0.992063PSPTO_1304 NC_004578.1 NA NA -1.529705 NAPSPTO_1340 NC_004578.1 NA NA NA NAPSPTO_1369 HrpL NC_004578.1 NA NA -0.779718 -1.132222PSPTO_1370 HrpL NC_004578.1 NA NA NA -2.185717PSPTO_1371 NC_004578.1 NA NA NA -2.250218PSPTO_1372 HrpL NC_004578.1 NA NA NA -2.553906PSPTO_1373 HrpL NC_004578.1 NA NA NA -0.947331PSPTO_1374 HrpL NC_004578.1 NA NA -1.315215 -1.805831PSPTO_1375 HrpL NC_004578.1 NA NA -1.710335 -2.787776PSPTO_1377 HrpL NC_004578.1 NA NA NA -1.229379PSPTO_1378 HrpL NC_004578.1 NA NA NA -2.09983PSPTO_1379 NC_004578.1 NA NA NA -1.531823PSPTO_1380 NC_004578.1 NA NA -1.138472 -1.012976

Page 105: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_1382 HrpL NC_004578.1 NA NA NA -0.546063PSPTO_1383 HrpL NC_004578.1 NA NA NA -0.910963PSPTO_1384 HrpL NC_004578.1 NA NA NA -0.882134PSPTO_1385 HrpL NC_004578.1 NA NA NA -1.21181PSPTO_1386 HrpL NC_004578.1 NA NA NA -2.402792PSPTO_1387 HrpL NC_004578.1 NA NA NA -0.878598PSPTO_1388 HrpL NC_004578.1 NA NA NA -0.880623PSPTO_1389 HrpL NC_004578.1 NA NA -0.833506 -1.248336PSPTO_1390 HrpL NC_004578.1 NA NA -0.830914 -1.152631PSPTO_1391 HrpL NC_004578.1 NA NA -0.892835 -1.251592PSPTO_1395 HrpL NC_004578.1 NA NA -0.875173 -1.661899PSPTO_1396 HrpL NC_004578.1 NA NA -1.031415 -1.635579PSPTO_1397 HrpL NC_004578.1 NA NA NA -2.095955PSPTO_1398 HrpL NC_004578.1 NA NA -0.8623 -1.172721PSPTO_1399 HrpL NC_004578.1 NA NA NA -1.235075PSPTO_1400 HrpL NC_004578.1 NA NA -2.311183 -3.49863PSPTO_1401 HrpL NC_004578.1 NA NA -1.468183 -2.321517PSPTO_1402 HrpL NC_004578.1 NA NA -1.106257 -1.733231PSPTO_1403 HrpL NC_004578.1 NA NA NA -2.13161PSPTO_1404 NC_004578.1 NA NA -0.993666 -1.23282PSPTO_1405 HrpL NC_004578.1 NA NA -0.698289 -1.063583PSPTO_1406 HrpL NC_004578.1 NA NA NA -1.546165PSPTO_1408 HrpL NC_004578.1 NA NA NA -1.652313PSPTO_1409 HrpL NC_004578.1 NA NA NA NAPSPTO_1429 NC_004578.1 NA NA NA 0.6044363PSPTO_1456 NC_004578.1 NA NA NA 0.4885487PSPTO_1475 RpoD NC_004578.1 NA NA NA 0.684324PSPTO_1509 NC_004578.1 NA NA NA NAPSPTO_1543 NC_004578.1 NA NA NA 0.4075718PSPTO_1544 NC_004578.1 NA NA NA 0.6113917PSPTO_1565 NC_004578.1 NA NA NA -0.751101PSPTO_1568 HrpL NC_004578.1 NA NA -2.54482 -2.88323PSPTO_1609 NC_004578.1 NA NA NA -0.968524PSPTO_1633 NC_004578.1 NA NA -0.819942 NAPSPTO_1708 NC_004578.1 NA NA NA -3.217811PSPTO_1721 RpoD NC_004578.1 NA -0.867269 NA -0.618334PSPTO_1724 NC_004578.1 NA NA NA -1.297375PSPTO_1749 NC_004578.1 NA NA NA 0.5692577PSPTO_1778 NC_004578.1 NA NA NA -1.100671PSPTO_1809 NC_004578.1 NA 0.5807564 NA NAPSPTO_1817 RpoD NC_004578.1 NA NA NA -0.882354PSPTO_1855 NC_004578.1 NA NA NA -2.353503PSPTO_1930 NC_004578.1 NA NA NA NAPSPTO_2047 NC_004578.1 NA NA NA -0.478379PSPTO_2049 NC_004578.1 -1.449981 NA NA NAPSPTO_2099 NC_004578.1 NA NA NA 0.6865337PSPTO_2105 HrpL NC_004578.1 NA NA NA -1.267981PSPTO_2128 NC_004578.1 NA NA NA -2.240612PSPTO_2130 NC_004578.1 NA NA NA -1.516483PSPTO_2133 Fur NC_004578.1 NA NA NA NAPSPTO_2134 PvdS NC_004578.1 NA NA NA NAPSPTO_2137 PvdS NC_004578.1 NA NA NA 5.0798361PSPTO_2139 PvdS NC_004578.1 NA NA NA NAPSPTO_2141 PvdS NC_004578.1 NA NA NA NAPSPTO_2142 PvdS NC_004578.1 NA NA NA NAPSPTO_2145 PvdS NC_004578.1 NA NA NA NAPSPTO_2146 PvdS NC_004578.1 NA NA NA NAPSPTO_2148 PvdS NC_004578.1 NA NA NA NA

Page 106: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_2152 PvdS NC_004578.1 NA NA 7.3330339 7.3720056PSPTO_2154 PvdS NC_004578.1 NA NA NA NAPSPTO_2155 PvdS NC_004578.1 NA NA NA NAPSPTO_2156 PvdS NC_004578.1 NA NA NA NAPSPTO_2195 NC_004578.1 NA NA NA NAPSPTO_2196 NC_004578.1 NA NA NA NAPSPTO_2198 NC_004578.1 NA NA NA NAPSPTO_2208 NC_004578.1 NA NA NA -0.154122PSPTO_2211 NC_004578.1 NA 0.4442514 NA NAPSPTO_2274 NC_004578.1 NA NA NA NAPSPTO_2275 NC_004578.1 NA NA NA NAPSPTO_2280 NC_004578.1 NA NA NA NAPSPTO_2298 NC_004578.1 NA NA NA 0.4531196PSPTO_2331 NC_004578.1 NA NA NA NAPSPTO_2338 NC_004578.1 NA NA NA NAPSPTO_2339 NC_004578.1 NA NA NA -1.222296PSPTO_2379 Fur, RpoD NC_004578.1 NA NA NA 0.3586306PSPTO_2380 RpoD NC_004578.1 NA NA NA 0.242557PSPTO_2381 RpoD NC_004578.1 NA NA NA 0.3514487PSPTO_2589 NC_004578.1 NA -2.507143 NA -2.080509PSPTO_2597 NC_004578.1 NA NA NA NAPSPTO_2598 NC_004578.1 NA NA NA NAPSPTO_2600 NC_004578.1 NA NA NA NAPSPTO_2601 NC_004578.1 NA NA NA NAPSPTO_2602 NC_004578.1 NA NA NA NAPSPTO_2603 NC_004578.1 NA NA NA NAPSPTO_2604 NC_004578.1 NA NA NA NAPSPTO_2605 Fur NC_004578.1 NA NA NA NAPSPTO_2638 NC_004578.1 NA NA NA -1.333573PSPTO_2678 HrpL NC_004578.1 NA NA NA -1.923894PSPTO_2680 NC_004578.1 NA NA NA -0.93577PSPTO_2691 NC_004578.1 NA NA -0.970912 -1.769909PSPTO_2702 NC_004578.1 NA NA NA -0.445932PSPTO_2705 NC_004578.1 NA NA NA NAPSPTO_2707 NC_004578.1 NA NA NA -0.38756PSPTO_2719 NC_004578.1 NA NA NA -0.759138PSPTO_2720 NC_004578.1 NA NA NA -1.082981PSPTO_2752 NC_004578.1 NA NA NA NAPSPTO_2806 NC_004578.1 NA NA NA -0.777017PSPTO_2844 NC_004578.1 NA NA NA -2.754938PSPTO_2845 NC_004578.1 NA NA NA -1.874569PSPTO_2850 NC_004578.1 NA NA NA -2.289521PSPTO_2853 NC_004578.1 NA NA NA -3.52925PSPTO_2904 NC_004578.1 NA NA NA NAPSPTO_3039 NC_004578.1 NA NA NA -0.537048PSPTO_3087 HrpL NC_004578.1 NA NA -0.541941 -0.957291PSPTO_3120 Fur NC_004578.1 NA NA 2.4163744 1.7678175PSPTO_3121 Fur NC_004578.1 NA NA NA 1.4718353PSPTO_3122 Fur NC_004578.1 NA NA 1.5228517 1.6000405PSPTO_3157 Fur NC_004578.1 NA NA NA NAPSPTO_3162 NC_004578.1 NA NA NA NAPSPTO_3269 Fur NC_004578.1 NA NA NA -1.140145PSPTO_3278 NC_004578.1 NA NA NA -0.980588PSPTO_3282 NC_004578.1 NA NA NA -0.707854PSPTO_3291 NC_004578.1 NA NA NA -1.515827PSPTO_3294 NC_004578.1 NA NA 4.6611429 4.9833611PSPTO_3323 NC_004578.1 NA NA NA NAPSPTO_3333 NC_004578.1 NA NA NA -0.890306

Page 107: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_3337 NC_004578.1 NA NA NA NAPSPTO_3349 NC_004578.1 NA NA NA 0.5159807PSPTO_3352 NC_004578.1 NA 1.409974 NA NAPSPTO_3353 NC_004578.1 NA NA NA -0.389868PSPTO_3355 NC_004578.1 NA NA NA -1.1227PSPTO_3364 NC_004578.1 NA NA NA NAPSPTO_3368 Fur NC_004578.1 NA NA NA NAPSPTO_3380 NC_004578.1 NA NA NA -1.28414PSPTO_3381 NC_004578.1 NA NA NA -1.897646PSPTO_3382 NC_004578.1 NA NA NA -0.850319PSPTO_3455 NC_004578.1 NA NA NA -1.009889PSPTO_3462 Fur NC_004578.1 NA NA NA NAPSPTO_3493 NC_004578.1 NA NA NA -1.208602PSPTO_3495 NC_004578.1 NA NA NA -0.880025PSPTO_3544 NC_004578.1 NA NA NA -0.992358PSPTO_3550 NC_004578.1 NA NA NA -0.716147PSPTO_3551 NC_004578.1 NA NA NA -0.48319PSPTO_3553 NC_004578.1 NA NA NA -0.815244PSPTO_3574 Fur NC_004578.1 NA NA 5.0776797 4.8034906PSPTO_3582 NC_004578.1 NA NA -3.225921 -2.726119PSPTO_3598 Fur NC_004578.1 NA NA 4.7406768 4.8797721PSPTO_3599 Fur NC_004578.1 NA NA 4.4080581 4.9908334PSPTO_3700 NC_004578.1 NA NA -0.803881 NAPSPTO_3733 RpoD NC_004578.1 NA 1.4586749 NA NAPSPTO_3815 NC_004578.1 NA NA NA NAPSPTO_3830 RpoD NC_004578.1 NA NA NA NAPSPTO_3836 RpoD NC_004578.1 NA 0.9193201 NA 0.6709119PSPTO_3893 NC_004578.1 NA NA NA -0.3774PSPTO_3925 NC_004578.1 NA NA NA -0.935669PSPTO_3959 NC_004578.1 NA NA NA -0.729666PSPTO_3972 NC_004578.1 NA NA NA 0.266933PSPTO_3973 NC_004578.1 NA NA NA 0.8334442PSPTO_3987 NC_004578.1 NA NA NA -0.561897PSPTO_4033 NC_004578.1 NA NA NA -0.597194PSPTO_4101 HrpL NC_004578.1 NA NA -0.731852 -1.258466PSPTO_4108 NC_004578.1 NA NA NA NAPSPTO_4136 NC_004578.1 NA NA 0.8332186 NAPSPTO_4145 NC_004578.1 NA NA 0.4615454 0.863006PSPTO_4159 Fur NC_004578.1 NA NA 6.426395 7.471834PSPTO_4160 NC_004578.1 NA NA -4.271013 -4.379085PSPTO_4168 NC_004578.1 NA NA NA -0.716317PSPTO_4173 NC_004578.1 NA NA NA -0.456383PSPTO_4174 NC_004578.1 NA NA NA -0.451413PSPTO_4224 NC_004578.1 NA NA NA 0.5829675PSPTO_4232 NC_004578.1 -4.230758 NA -4.283955 NAPSPTO_4233 NC_004578.1 NA NA -3.148023 NAPSPTO_4234 NC_004578.1 NA NA -2.234802 NAPSPTO_4285 NC_004578.1 NA NA NA -2.361196PSPTO_4297 NC_004578.1 NA -1.412129 NA -1.894108PSPTO_4306 NC_004578.1 NA NA NA NAPSPTO_4331 HrpL NC_004578.1 NA NA NA -0.575976PSPTO_4332 NC_004578.1 NA NA -1.10646 NAPSPTO_4333 NC_004578.1 NA NA NA -1.630766PSPTO_4339 NC_004578.1 NA NA NA -0.893949PSPTO_4358 NC_004578.1 NA NA NA -0.496201PSPTO_4363 RpoD NC_004578.1 NA NA NA -1.449999PSPTO_4366 Fur NC_004578.1 NA NA 5.6377242 2.2418911PSPTO_4367 Fur NC_004578.1 NA NA 2.994826 2.2354584

Page 108: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_4368 Fur NC_004578.1 NA NA 2.57355 0.985238PSPTO_4369 Fur NC_004578.1 NA NA 1.6313637 0.8441955PSPTO_4380 NC_004578.1 NA NA NA NAPSPTO_4381 NC_004578.1 NA NA 1.8012265 2.1540737PSPTO_4407 NC_004578.1 NA 0.55374 NA NAPSPTO_4423 NC_004578.1 NA 0.8461829 NA NAPSPTO_4442 RpoD NC_004578.1 NA 1.397263 NA 0.7856238PSPTO_4444 RpoD NC_004578.1 NA NA NA NAPSPTO_4452 RpoD NC_004578.1 NA 0.3322938 NA NAPSPTO_4456 NC_004578.1 NA NA NA 0.8525176PSPTO_4473 NC_004578.1 NA 0.6535008 NA NAPSPTO_4484 RpoN NC_004578.1 NA NA -0.599805 NAPSPTO_4494 RpoD NC_004578.1 NA 1.2938911 NA NAPSPTO_4499 RpoD NC_004578.1 NA NA NA 0.3371682PSPTO_4503 NC_004578.1 NA NA NA NAPSPTO_4507 NC_004578.1 NA NA NA -0.897708PSPTO_4530 Fur NC_004578.1 NA NA NA -0.707174PSPTO_4557 NC_004578.1 NA NA NA NAPSPTO_4558 NC_004578.1 NA NA 0.7495851 NAPSPTO_4560 NC_004578.1 NA NA NA -1.23534PSPTO_4562 NC_004578.1 NA NA NA NAPSPTO_4573 NC_004578.1 NA 0.5384356 NA NAPSPTO_4578 NC_004578.1 NA NA NA 1.6063946PSPTO_4582 NC_004578.1 NA NA NA NAPSPTO_4588 HrpL NC_004578.1 NA NA NA -2.085412PSPTO_4589 HrpL NC_004578.1 NA NA -0.958698 -1.580561PSPTO_4597 HrpL NC_004578.1 NA NA NA -1.8858PSPTO_4599 HrpL NC_004578.1 NA NA -0.854476 -1.418736PSPTO_4610 NC_004578.1 NA NA NA 1.5505564PSPTO_4611 NC_004578.1 NA NA NA 1.593792PSPTO_4646 NC_004578.1 NA NA NA -1.740455PSPTO_4647 NC_004578.1 NA NA NA -3.151012PSPTO_4648 NC_004578.1 NA NA NA NAPSPTO_4685 NC_004578.1 NA NA NA -0.257303PSPTO_4686 NC_004578.1 NA NA NA -0.328762PSPTO_4687 NC_004578.1 NA NA NA -0.411068PSPTO_4690 NC_004578.1 NA NA NA -0.329838PSPTO_4691 HrpL NC_004578.1 NA NA NA -2.28565PSPTO_4703 HrpL NC_004578.1 NA NA -1.067705 -1.018289PSPTO_4704 NC_004578.1 NA NA -1.306811 -1.312865PSPTO_4718 HrpL NC_004578.1 NA NA -0.984917 -1.992004PSPTO_4720 HrpL NC_004578.1 NA NA NA -0.507764PSPTO_4721 HrpL NC_004578.1 NA NA NA -0.530916PSPTO_4727 HrpL NC_004578.1 NA NA NA -3.526454PSPTO_4733 HrpL NC_004578.1 NA NA NA -1.930883PSPTO_4762 NC_004578.1 NA NA NA NAPSPTO_4766 NC_004578.1 NA NA NA -1.070108PSPTO_4776 HrpL NC_004578.1 NA NA -0.704359 -0.852561PSPTO_4807 NC_004578.1 NA NA NA 0.4328318PSPTO_4933 RpoD NC_004578.1 NA NA NA 0.2722594PSPTO_4943 NC_004578.1 NA NA NA 0.7293258PSPTO_4955 RpoD NC_004578.1 NA NA NA -0.637728PSPTO_4956 NC_004578.1 NA NA NA NAPSPTO_5046 NC_004578.1 NA 0.5763849 NA NAPSPTO_5087 NC_004578.1 NA -1.321346 NA NAPSPTO_5141 NC_004578.1 NA 0.5035041 NA NAPSPTO_5147 NC_004578.1 NA NA NA -0.509583PSPTO_5154 NC_004578.1 NA NA NA 0.3378382

Page 109: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO_5255 NC_004578.1 NA NA NA -0.761021PSPTO_5256 NC_004578.1 NA NA NA -1.578395PSPTO_5310 NC_004578.1 NA NA 0.3602312 NAPSPTO_5325 RpoD NC_004578.1 NA 0.9899235 NA NAPSPTO_5351 NC_004578.1 NA NA NA NAPSPTO_5353 HrpL NC_004578.1 NA NA NA NAPSPTO_5354 HrpL NC_004578.1 NA NA NA -1.151489PSPTO_5355 NC_004578.1 NA NA NA -0.677055PSPTO_5377 NC_004578.1 NA 2.5588455 NA 2.8623793PSPTO_5378 NC_004578.1 NA 3.8950923 NA 3.2728285PSPTO_5379 NC_004578.1 NA 2.5138799 NA 1.6877617PSPTO_5380 NC_004578.1 NA 3.2082837 NA 2.8727084PSPTO_5381 NC_004578.1 NA 3.7296646 NA 3.0217049PSPTO_5407 NC_004578.1 NA NA NA -1.42497PSPTO_5433 NC_004578.1 NA NA NA NAPSPTO_5466 NC_004578.1 NA NA NA -0.73141PSPTO_5474 NC_004578.1 NA NA NA NAPSPTO_5507 NC_004578.1 NA NA NA NAPSPTO_5517 NC_004578.1 NA NA NA -0.759383PSPTO_5522 NC_004578.1 NA NA NA -0.501934PSPTO_5614 RpoD NC_004578.1 NA NA NA 0.5010452PSPTO_5620 HrpL NC_004578.1 NA NA NA NAPSPTO_5621 NC_004578.1 NA NA NA -1.50138PSPTO_5622 HrpL NC_004578.1 NA NA NA -0.47389

PSPTO_A0008 NC_004633.1 NA NA NA -0.660665PSPTO_A0009 NC_004633.1 NA NA NA -0.631442PSPTO_A0011 NC_004633.1 NA NA NA -1.183121PSPTO_A0012 HrpL NC_004633.1 NA NA -0.744616 -1.373186PSPTO_A0017 HrpL NC_004633.1 NA NA -0.666939 -0.898187PSPTO_A0018 HrpL NC_004633.1 NA NA NA -0.885862PSPTO_A0019 HrpL NC_004633.1 NA NA NA -1.21726PSPTO_B0005 HrpL NC_004632.1 NA NA -0.598869 -0.896596PSPTO_B0010 NC_004632.1 NA NA NA NAPSPTO_B0012 NC_004632.1 NA NA NA NAPSPTO_B0025 NC_004632.1 NA NA NA -0.648474PSPTO_B0026 NC_004632.1 NA NA NA -0.777345PSPTO_B0027 NC_004632.1 NA NA NA -0.68997

small RNA cobalamin-4 NC_004578.1 NA NA 2.7252975 1.6521049NC_004578.1 NA NA NA 0.6604825

Fur NC_004578.1 NA NA 7.7506725 6.7324644small RNA P1

small RNA prrF2

Page 110: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

b-/c- b-/b+ c-/c+ b+/c+ nameNA NA NA NA recFNA NA NA NANA NA -2.569791 NA hopK1NA NA -1.837164 NA hopY1NA NA NA 4.6206006NA NA 5.2431938 NA tonB-1NA NA 6.4724107 NA exbD-1NA 7.4606887 8.8815456 NA exbB-1NA NA NA -0.678637NA NA NA 1.1990988 osmCNA NA NA 0.8234983NA NA NA 1.1969337NA NA -0.875973 NANA NA NA NANA NA NA NA iucDNA NA NA -0.478003 glnKNA NA NA 1.3124878NA NA NA NANA NA NA -0.969471NA NA NA 2.3986034NA NA NA 2.7213842NA NA NA NA cysTNA 4.117592 3.2081509 NANA NA NA -0.676925 ompRNA NA NA 2.7292792NA NA NA -1.307261NA NA NA -0.40516 iaaLNA NA NA NANA NA NA -1.232993NA NA -2.096007 NA shcFNA NA -2.725466 NANA NA NA NA rpsUNA NA NA NANA NA NA NANA NA NA -1.114781NA NA NA NA apaHNA NA NA NA pdxANA NA NA -1.563118NA NA NA -1.576779NA NA -1.522258 NA hopH1NA NA -1.330995 NA hopC1NA NA NA NA trpCNA NA -1.478206 NA speDNA NA -1.333644 NANA NA NA NA rplKNA NA NA NA rpsLNA NA NA NA rplWNA NA NA NA rplXNA NA NA NA rplENA NA NA NA rplRNA NA NA NA rpmJNA NA NA 0.2722516 rpsMNA NA NA NA rpsKNA NA NA 0.272706 rpoANA NA -4.392562 NANA NA NA NA

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 111: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NA NANA NA NA NANA NA NA NA eutBNA NA NA -0.710799NA NA 0.8415704 NA fecBNA NA NA -1.192894 recCNA NA -0.98789 NA ileSNA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA -2.631302 -1.288898NA NA -1.869806 -0.941171 hopAJ1NA NA NA -0.733131NA NA -1.188587 NANA NA NA NANA NA NA NANA NA -3.60018 NANA NA -1.136097 -0.458249 hopD1NA NA -1.889711 -0.964677 hopQ1-1NA NA -1.250294 -1.036829 hopR1NA NA 1.9722201 NANA NA NA -0.46868NA NA NA NA terZNA NA NA -0.364826 terDNA NA -0.587486 -0.712299NA NA -0.949544 -1.075107 fruKNA NA NA NA pgiNA NA -0.60022 NA panBNA NA -0.716451 NANA NA NA NA pthNA NA NA 1.3432154NA NA NA -1.051331 alkKNA NA NA NANA NA NA NANA NA NA -3.114861NA NA NA -0.499937 gap-1NA NA NA -0.751593 eddNA NA NA NA glkNA NA NA -0.333095NA NA NA NA oprBNA NA NA -0.588118 zwf-1NA NA NA -0.584589 pglNA NA NA -1.215476 eda-1NA NA NA 1.4541544NA NA NA -0.925166NA NA -1.316473 NANA NA -2.227402 NA hopN1NA NA -1.323891 NANA NA -2.561653 NA hopAA1-1NA NA NA -0.607316 hrpW1NA NA -2.115172 NA shcMNA NA -2.822233 NA hopM1NA NA -1.173796 NA avrE1NA NA -2.406927 NANA NA -2.414211 NA hrpRNA NA -1.340359 NA hrpS

Page 112: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA NA NA hrpZ1NA NA -1.34125 NA hrpB(Pto)NA NA -1.311128 NA hrcJNA NA -1.611665 NA hrpDNA NA -2.790877 NA hrpENA NA -1.620227 NA hrpFNA NA -1.393513 NA hrpGNA NA -1.425796 NA hrcCNA -0.888026 -1.321 NA hrpTNA -1.119342 -1.779791 NA hrpVNA NA -1.751173 NA hrcRNA -1.419277 -1.888265 NA hrcQbNA NA -2.364174 NA hrcQaNA NA -1.652615 NA hrpPNA NA -1.735737 NA hrpONA NA -4.469206 -1.187447 hrcNNA NA -2.537096 -0.853334 hrpQNA NA -2.053826 -0.626974 hrcVNA NA -2.508559 -1.311557 hrpJNA NA -1.729669 NA hrpLNA NA -0.964165 NA hrpK1NA NA -1.521306 NA hopB1NA NA -2.976955 NANA NA -2.312568 NANA NA NA NANA NA NA NA cumANA NA NA 0.6063817 trmDNA NA -0.531011 NA adkNA NA NA NANA NA NA NA lpxDNA NA NA -1.153686 rpoSNA NA -4.379087 NA hopAF1NA NA -0.761407 NANA NA NA 1.7586162 asnBNA NA NA NA cobONA NA NA -0.696213NA NA NA -1.253753NA NA NA NA cmkNA NA NA NA htpXNA NA NA NA ispZNA NA NA NANA NA NA NANA NA NA -0.996594 cynSNA NA -1.005385 NANA NA NA NANA NA NA NANA NA -1.705116 NANA NA -2.247789 NANA NA -1.571067 NANA NA 8.6313434 NANA NA 7.2229953 NANA NA 9.0235798 NANA NA 1.2342227 NANA NA 3.9797651 NANA NA 4.4037076 NANA NA 6.4421761 NANA NA 8.3829504 NANA NA 7.5205386 NA

Page 113: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA 11.478055 NANA NA 8.953826 NANA NA 3.4822469 NANA NA 8.3864441 NANA NA -0.79397 NA sdhCNA NA -0.863482 NANA NA -0.447865 NA sdhBNA NA NA NA htpGNA NA NA NA fabANA NA NA -1.035173NA NA -0.731734 NA aroF-1NA NA -1.783935 NA cysHNA NA NA NANA NA NA -0.830807NA NA -3.314767 NA pcaHNA NA -1.724496 NA pcaGNA NA NA 0.2979876 infCNA NA NA NA rpmINA NA NA NA rplTNA NA NA -2.097998NA NA 8.2557731 NA irp5NA NA 9.2882023 NA irp4NA NA 10.3148 NA irp1NA NA 9.8562613 NANA NA 10.275206 NANA NA 8.8035334 NANA NA 7.144291 NANA NA 9.3737924 NANA NA NA NA abPNA NA -1.863967 NA hopP1NA NA NA NA gabD-3NA -0.99366 NA NANA NA NA NA xylBNA NA NA -0.555793NA NA NA -0.554632NA NA -1.032754 NANA NA NA -1.004752 nudCNA NA NA -0.551873 tpxNA NA NA NANA NA NA NANA NA NA NANA NA NA -1.701148NA NA NA NANA NA -1.383172 NA vanANA NA NA NANA NA -1.072279 -0.41535 hopAB2NA NA 2.1399956 NANA NA 1.9114979 NA zwf-2NA 1.846405 2.0177668 NA gndNA NA 7.3413133 NANA NA -1.017873 NANA NA NA NA pstSNA NA NA -1.133383NA NA NA -0.903342NA NA NA -1.892764NA NA 6.0026651 NANA NA NA -1.077138NA NA NA -0.835678

Page 114: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA -1.19748 -1.132503NA NA NA NA ftsKNA NA NA NA infANA NA NA -0.55455 clpANA NA NA NANA NA -0.701358 -0.712302 aceANA NA -1.82099 NA nuoENA NA -1.707997 NANA NA -2.138914 NANA NA -1.220539 NANA NA NA -1.082239NA NA 5.4455626 NANA NA NA -1.424707NA NA NA -1.038047NA NA NA -1.045906NA NA NA -0.856498 fahANA NA NA -0.717647 hmgANA NA NA -1.104574 hppDNA NA 6.0741522 NANA NA -3.149391 NA katBNA NA 5.9791688 NANA 4.3661633 6.006367 NANA NA NA NANA NA -1.309743 NA folD-2NA NA -0.377489 NA accDNA NA -0.808017 NA fabFNA NA NA 0.6143344NA NA NA NANA NA NA -1.45071NA NA -1.263039 NA nadANA NA NA NA tolBNA NA NA NA tolANA NA NA NA oprDNA NA NA NA recANA NA -1.202933 -0.526614 hopAK1NA NA NA -0.546846NA NA NA NANA NA NA NA capBNA NA 8.6726328 NANA NA -7.164039 NA bfrNA NA NA NA glpKNA NA NA NANA NA NA NANA NA NA NA rpoENA NA NA 4.2967204NA NA NA 3.2280417NA NA NA 2.3846269NA NA NA NA adhBNA NA NA -1.902474NA NA NA -1.983058 pcaTNA NA -0.778112 NA hopE1NA NA -2.257178 NANA NA -1.637949 NANA NA NA NANA NA NA NANA NA -2.357771 NA sodBNA NA 2.8906637 NANA 3.1189294 NA NA

Page 115: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA 2.6079728 NA -1.588312NA 1.5948477 1.0430709 NANA NA NA -1.170299 fabGNA NA 2.6062957 NANA NA NA NA murCNA NA NA NA sspBNA NA NA NANA NA -0.5009 NANA NA NA NANA NA NA NANA NA NA NA gatCNA NA NA 1.070266NA NA -0.940087 NA tpiANA NA NA NANA NA NA 0.6466547 dapBNA NA NA NA recNNA NA -0.530731 -0.518222 katGNA NA NA -1.201284NA NA NA -1.541535NA NA NA -2.745063NA NA -2.410928 NANA NA NA NANA NA NA 2.5213387NA NA NA -0.680931NA NA -1.97661 NA hopS2NA NA -1.421445 NA shcS2NA NA -3.303099 NA hopS1NA NA -1.609763 -0.56426 shcS1NA NA NA NANA NA NA 1.6315049NA NA NA NANA NA -4.164426 NA cioBNA NA -4.224823 NA cioANA NA NA NA cfa5NA NA NA NA cfa6NA NA NA NA cfa7NA NA NA NA cfa9NA NA NA NA hopAD1NA NA -2.393651 NA hopAQ1NA NA -2.804716 NA corRNA NA -2.01319 NA hopAA1-2NA NA NA NA hopV1NA NA NA NA shcVNA NA -3.259571 NA hopG1NA NA -2.561408 NANA NA NA -1.795079NA NA -0.884254 NANA NA -1.05818 NA hopI1NA NA NA NANA NA NA NA rpsFNA NA NA NA miaANA NA NA NA psdNA NA -0.826646 NANA NA NA NANA NA NA NA mdcANA NA -0.563034 NA hslUNA NA NA -0.636368NA NA NA NA hisE

Page 116: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA -0.721661 NA cynTNA NA -1.347329 NANA NA NA NANA NA -0.784315 NANA NA NA 1.719238NA NA -2.579072 NA shcANA NA -1.565909 NA hopA1NA NA -1.237459 NANA NA NA 2.2862165NA NA NA 3.0034822NA NA NA NANA NA NA 2.5088942NA NA NA 2.3561983NA NA NA NANA NA 0.6246498 NANA NA NA NANA NA -0.957503 NA rubANA NA NA 1.1852055NA NA NA NANA NA NA NANA NA NA NA rnpANA NA -2.949454 NANA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA -1.478059 NA HopX1NA NA -1.306641 NA shc01NA NA -0.881881 -0.525359 hopO1-1NA NA -1.70248 NA hopT1-1NA NA -0.974053 NA plcA2NA NA NA -0.40954NA NA -1.157763 NANA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA NA NANA NA 8.2707426 NA prrF2

Page 117: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

annotationrecombination protein F

DNA-binding proteintype III effector HopK1type III effector HopY1

citrate transportertonB protein

TonB system transport protein ExbDTonB system transport protein ExbB

bacterial extracellular solute-binding protein, family 5osmotically inducible protein

hypothetical proteinhypothetical protein

sulfatase family proteinhypothetical protein

L-lysine 6-monooxygenasenitrogen regulatory protein P-II

hypothetical proteinhypothetical proteinhypothetical proteinhypothetical proteinhypothetical protein

sulfate ABC transporter, permease protein CysTiron ABC transporter, periplasmic iron-binding protein

DNA-binding response regulator OmpRhypothetical protein

oxidoreductase, aldo keto reductase familyindoleacetate-lysine ligase

peptidase, M16 familyhypothetical protein

type III chaperone protein ShcFpeptidase, M20 M25 M40 family

30S ribosomal protein S21SpoVR like family protein

hypothetical proteinhypothetical protein

diadenosinetetraphosphatase4-hydroxythreonine-4-phosphate dehydrogenase

autotransporting lipase, GDSL familytranscriptional regulator PrtN, putative

type III effector HopH1type III effector HopC1

indole-3-glycerol-phosphate synthaseS-adenosylmethionine decarboxylase proenzyme

hypothetical protein50S ribosomal protein L1130S ribosomal protein S1250S ribosomal protein L2350S ribosomal protein L2450S ribosomal protein L5

50S ribosomal protein L1850S ribosomal protein L3630S ribosomal protein S1330S ribosomal protein S11

DNA-directed RNA polymerase alpha subunitbacterioferritin

lipopolysaccharide biosynthesis protein, putative

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 118: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

outer membrane protein OmpWglutathione S-transferase family protein

ethanolamine ammonia-lyase, heavy subunitaldehyde dehydrogenase family protein

iron(III) dicitrate transport system, periplasmic iron-binding protein FecBexodeoxyribonuclease V, gamma subunit

isoleucyl-tRNA synthetasealcohol dehydrogenase, zinc-containing

ribD C-terminal domain proteinhypothetical proteinhypothetical protein

major facilitator family transporterhypothetical protein

type III effector HopAJ1dnaK suppressor protein, putative

ParA family proteinamidinotransferase family protein

nikkomycin biosynthesis domain proteinhypothetical protein

type III effector HopD1type III effector HopQ1-1type III effector HopR1

methyl-accepting chemotaxis proteintype IV pilus biogenesis proteintellurium resistance protein TerZtellurium resistance protein TerD

phosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components1-phosphofructokinase

glucose-6-phosphate isomerase3-methyl-2-oxobutanoate hydroxymethyltransferase

carbonic anhydrasepeptidyl-tRNA hydrolase

amino acid ABC transporter, periplasmic amino acid-binding proteinacyl-CoA synthaseompA family protein

transcriptional regulator, AraC familymembrane protein

glyceraldehyde-3-phosphate dehydrogenasephosphogluconate dehydratase

glucokinaseDNA-binding response regulator

porin Bglucose-6-phosphate 1-dehydrogenase

6-phosphogluconolactonaseketo-hydroxyglutarate-aldolase keto-deoxy- phosphogluconate aldolase

hypothetical proteincarbonic anhydrase

conserved effector locus proteintype III effector HopN1

conserved effector locus proteintype III effector HopAA1-1

type III helper protein HrpW1type III chaperone ShcMtype III effector HopM1

type III effector protein AvrE1membrane-bound lytic murein transglycosylase D, putative

type III transcriptional regulator HrpRtype III transcriptional regulator HrpS

Page 119: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

type III helper protein HrpZ1type III secretion protein HrpB(Pto)

type III secretion protein HrcJtype III secretion protein HrpDtype III secretion protein HrpEtype III secretion protein HrpFtype III secretion protein HrpG

outer-membrane type III secretion protein HrcCtype III secretion protein HrpT

negative regulator of hrp expression HrpVtype III secretion protein HrcR

type III secretion protein HrcQbtype III secretion protein HrcQatype III secretion protein HrpPtype III secretion protein HrpO

type III secretion cytoplasmic ATPase HrcNtype III secretion protein HrpQtype III secretion protein HrcVtype III secretion protein HrpJ

RNA polymerase sigma factor HrpLtype III helper protein HrpK1

type III effector HopB1hypothetical proteinhypothetical proteinhypothetical proteinmulticopper oxidase

tRNA (guanine-N(1)-)-methyltransferaseadenylate kinase

outer membrane protein OmpH, putativeUDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase

RNA polymerase sigma factortype III effector HopAF1

hypothetical proteinasparagine synthetase, glutamine-hydrolyzing

cob(I)yrinic acid a,c-diamide adenosyltransferasehypothetical proteinhypothetical protein

cytidylate kinaseheat shock protein HtpX

putative intracellular septation proteinaromatic amino acid permease

TonB-dependent receptor, putativecyanate hydratase

HAD-superfamily hydrolasehypothetical protein

helicase SNF2 family domain proteinthiamine biosynthesis lipoprotein, putative

response regulatorDNA-binding response regulator, LuxR family

RNA polymerase sigma-70 factorpyoverdine synthetase, thioesterase component

MbtH-like proteincation ABC transporter, permease protein

cation ABC transporter, periplasmic cation-binding proteinhypothetical protein

iron-regulated membrane protein, putativepyoverdine biosynthesis regulatory gene, putative

pyoverdine sidechain peptide synthetase II, D-Asp-L-Thr component

Page 120: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

TonB-dependent siderophore receptor, putativehypothetical protein

aminotransferase, class Vrenal dipeptidase family protein

succinate dehydrogenase, cytochrome b556 subunitsuccinate dehydrogenase, hydrophobic membrane anchor protein

succinate dehydrogenase catalytic subunitheat shock protein 90

3-hydroxydecanoyl-ACP dehydratasehypothetical protein

3-deoxy-7-phosphoheptulonate synthasephosphoadenosine phosphosulfate reductase

RNA polymerase sigma-70 factordeoxyguanosinetriphosphate triphosphohydrolase

protocatechuate 3,4-dioxygenase, beta subunitprotocatechuate 3,4-dioxygenase, alpha subunit

translation initiation factor IF-350S ribosomal protein L3550S ribosomal protein L20

hypothetical proteinyersiniabactin synthetase, salycilate ligase component

yersiniabactin synthetase, thioesterase componentyersiniabactin polyketide non-ribosomal peptide synthetase

hypothetical proteinyersiniabactin non-ribosomal peptide synthetaseABC transporter, ATP-binding permease proteinABC transporter, ATP-binding permease proteinTonB-dependent siderophore receptor, putative

L-arabinose ABC transporter, periplasmic L-arabinose-binding proteintype III helper protein HopP1

succinate-semialdehyde dehydrogenasemembrane protein, TerC family

xylulokinasemannitol ABC transporter, permease protein

mannitol ABC transporter, periplasmic mannitol-binding proteinenoyl-CoA hydratase

NADH pyrophosphatasethiol peroxidase

dienelactone hydrolase family proteinhypothetical proteinhypothetical proteinhypothetical protein

TonB-dependent receptor, putativevanillate O-demethylase, oxygenase subunit

alcohol dehydrogenase, zinc-containingtype III effector HopAB2

Cof-like hydrolase family proteinglucose-6-phosphate 1-dehydrogenase

6-phosphogluconate dehydrogenasehypothetical proteinhypothetical protein

phosphate ABC transporter, periplasmic phosphate-binding proteinhypothetical proteinlipoprotein, putative

methyl-accepting chemotaxis proteinTonB-dependent siderophore receptor, putative

aldehyde dehydrogenase family proteinhypothetical protein

Page 121: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

hypothetical proteincell division protein FtsK

translation initiation factor IF-1ATP-dependent clp protease, ATP-binding subunit ClpA

cold shock domain family proteinisocitrate lyase

ATP synthase subunit Esensor histidine kinase

DNA-binding response regulatorlipoprotein, putative

3-oxoacid CoA-transferase, subunit A familyTonB-dependent siderophore receptor

iolH proteiniolD protein

hypothetical proteinfumarylacetoacetase

homogentisate 1,2-dioxygenase4-hydroxyphenylpyruvate dioxygenase

TonB-dependent siderophore receptor, putativecatalase

dyp-type peroxidase family proteinhypothetical protein

oxidoreductase, aldo keto reductase familymethylenetetrahydrofolate dehydrogenase methenyltetrahydrofolate cyclohydrolase

acetyl-CoA carboxylase beta subunit3-oxoacyl-(acyl carrier protein) synthase

hypothetical proteinglyoxalase, putative

gas vesicle protein, putativequinolinate synthetase

translocation protein TolB precursortolA protein

porin Drecombinase A

type III effector HopAK1high-affinity branched-chain amino acid ABC transporter, periplasmic amino acid-binding protein

amino acid ABC transporter, periplasmic amino acid-binding proteincold shock protein CapB

bacterioferritin-associated ferredoxinbacterioferritinglycerol kinase

amino acid ABC transporter, permease proteinamino acid ABC transporter, ATP-binding protein

RNA polymerase sigma-70 factorTctC protein, putative

membrane protein TctB, putativemembrane protein TctA, putative

alcohol dehydrogenase IIhypothetical protein

dicarboxylic acid transport proteintype III effector HopE1

hypothetical proteinmoxR protein, putative

fumarate hydratase, class I, putativeoxidoreductase, FAD FMN-binding

superoxide dismutase, Feiron-regulated protein A, putative

lipoprotein, putative

Page 122: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

lipoprotein, putativelipoprotein, putative

3-ketoacyl-(acyl-carrier-protein) reductasehypothetical protein

UDP-N-acetylmuramate--L-alanine ligasestringent starvation protein B

toluene tolerance protein, putativetoluene tolerance protein, putative

ABC transporter, ATP-binding proteinhypothetical protein

aspartyl glutamyl-tRNA amidotransferase subunit Chypothetical protein

triosephosphate isomerasehypothetical protein

dihydrodipicolinate reductaseDNA repair protein RecNcatalase peroxidase HPI

peptide ABC transporter, periplasmic peptide-binding proteindipeptide ABC transporter, periplasmic dipeptide-binding protein, putative

outer membrane porin, OprD familydipeptide ABC transporter, permease protein

hypothetical proteinglycine betaine carnitine choline ABC transporter, permease protein

hypothetical proteintype III effector HopS2

type III chaperone ShcS2type III effector HopS1

type III chaperone ShcS1hypothetical proteinhypothetical proteinhypothetical protein

cyanide-insensitive terminal oxidase CioBcyanide-insensitive terminal oxidase CioA

coronafacic acid synthetase, ligase componentcoronafacic acid polyketide synthase I

coronafacic acid polyketide synthetase IICFA synthetase, thioesterase component

type III effector HopAD1type III effector HopAQ1

DNA-binding response regulator CorRtype III effector HopAA1-2

type III effector HopV1type III chaperone ShcVtype III effector HopG1

hypothetical proteinvon Willebrand factor type A domain protein

hypothetical proteintype III effector HopI1

metal ion transporter, putative30S ribosomal protein S6

tRNA delta(2)-isopentenylpyrophosphate transferasephosphatidylserine decarboxylase

hypothetical proteinhypothetical protein

malonate decarboxylase, alpha subunitATP-dependent protease ATP-binding subunit

polyhydroxyalkanoate granule-associated protein PhaFphosphoribosyl-ATP pyrophosphatase

Page 123: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

carbonic anhydrasesulfate transporter family protein

glutamine synthetaseglutaredoxin

lipoprotein, putativetype III chaperone protein ShcA

type III effector HopA1hypothetical proteinhypothetical proteinhypothetical proteinhypothetical protein

allophanate hydrolase, putativebiotin carboxylase biotin carboxyl carrier protein

oxidoreductase, molybdopterin-bindinghypothetical proteinhypothetical protein

rubredoxinacetyltransferase, GNAT family

hypothetical proteinhypothetical protein

ribonuclease PPSPTO_5620PSPTO_5621PSPTO_5622

partion protein, ParB familyATPase, ParA familyresolvase, putative

type III effector HopX1type III chaperone ShcO1type III effector HopO1-1type III effector HopT1-1

phosphoesterase family proteinmajor facilitator family transporter

hypothetical proteinhypothetical proteinhypothetical proteinhypothetical protein

within intergenic region 3679906-3680084within intergenic region 6038188-6038782within intergenic region 3549362-3549773

Page 124: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

notesRequired for DNA replication; binds preferentially to single-stranded, linear DNA

identified by match to PFAM protein family HMM PF01381previously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putative

Previously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to GP:14595286, and GP:14595286; identified by sequence similarity; putativesimilar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putative

similar to GP:14595284; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00496

similar to SP:P23929, GB:M16447, GB:X04882, SP:P09417, PID:181553, and PID:30819; identified by sequence similarity; putativesimilar to GP:9945860; identified by sequence similarity; putative

similar to GP:15978663; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00884

identified by Glimmer2; putativesimilar to SP:P11295; identified by sequence similarity; putative

similar to GP:2735324; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00149

identified by Glimmer2; putative

identified by Glimmer2; putativesimilar to SP:P33159, GB:X68014, and PID:40807; identified by sequence similarity; putative

similar to SP:Q9HT89; identified by sequence similarity; putativesimilar to SP:Q46851, GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

similar to SP:P18204, GB:J04031, SP:P11586, and PID:307178; identified by sequence similarity; putativesimilar to GP:9946224; identified by sequence similarity; putative

similar to GP:9946369, and GP:9946369; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF01546Interacts with residues in the 16S gene, protecting the stem-loop structure

identified by match to PFAM protein family HMM PF04293identified by match to PFAM protein family HMM PF04285

similar to SP:P77391; identified by sequence similarity; putativeCatalyzes the hydrolysis of P1,P4-bis(5 -adenosyl) tetraphosphate

An essential cofactor for many enzymes responsible for the metabolic conversions of amino acids

previously known as HopPtoH (PMID 12032338; Petnicki-Ocwieja et al, 2002).previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586

Catalyzes the conversion of 1-(2-carboxyphenylamino)1-deoxy-D-ribulose 5 phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate during the biopsynthesis of tryptophanS-adenosylmethionine provides the aminopropyl moiety required for spermidine biosynthesis from putrescine

binds directly to 23S ribosomal RNAImportant for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s

Binds signal recoginition particle and trigger factor at the peptide exit area on the 50S ribosomeFound in the ribonucleoprotein core and is involved in the early assembly of the 50S subunit

Mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberancebinds 5S rRNA

Ribosomal protein L36 is the smallest protein from the large subunit of the prokaryotic ribosomeLocated at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA

located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosomeCatalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log 2.

Page 125: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile)identified by match to TIGR protein family HMM TIGR01751

similar to GB:S69136, GB:S69198, GB:M28594, and PID:292763; identified by sequence similarity; putativeAlso known as ORF24 (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to TIGR protein family HMM TIGR01449

identified by Glimmer2; putativesimilar to GB:U01783, and PID:409855; identified by sequence similarity; putative

similar to SP:P77262; identified by sequence similarity; putativepreviously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putative

similar to SP:P18274, GB:M25499, SP:P16588, and PID:155251; identified by sequence similarity; putativesimilar to PIR:B42465; identified by sequence similarity; putative

similar to GP:5919222, GB:M13699, GB:D00025, GB:X69706, GB:M13536, GB:X04136, GB:X04137, GB:X04138, SP:P00450, PID:1335036, PID:1335037, PID:1666064, and PID:180249; identified by sequence similarity; putativesimilar to GP:14030855; identified by sequence similarity; putative

Also known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putative

Previously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

similar to GP:4235392; identified by sequence similarity; putative

similar to SP:Q52353; identified by sequence similarity; putativesimilar to SP:P18781; identified by sequence similarity; putative

catalyzes the formation of D-fructose 6-phosphate from D-glucose 6-phosphateCatalyzes the first committed step in the biosynthesis of pantothenate

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putativeEnables the recycling of peptidyl-tRNAs produced at termination of translation

Activates fatty acids by binding to coenzyme Asimilar to GP:5123490; identified by sequence similarity; putative

similar to GP:13936369; identified by sequence similarity; putativesimilar to GP:13936368; identified by sequence similarity; putative

catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphatecatalyzes the formation of 2-dehydro-3-deoxy-6-phospho-D-gluconate from 6-phospho-D-gluconate

catalyzes the conversion of ATP and D-glucose to ADP and D-glucose 6-phosphate

catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphatecatalyzes the formation of 6-phospho-D-gluconate from 6-phospho-D-glucono-1,5-lactone

catalyzes the formation of pyruvate and glyoxylate from 4-hydroxy-2-oxoglutarate; or pyruvate and D-glyceraldehyde 3-phosphate from 2-dehydro-3-deoxy-D-glyconate 6-phosphate

identified by match to TIGR protein family HMM TIGR01409similar to GP:8037800; identified by sequence similarity; putative

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586similar to GP:8037798, SP:P32109, GB:U15124, and PID:563996; identified by sequence similarity; putative

previously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987similar to GP:3694999, and GP:8037796; identified by sequence similarity; putative

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to SP:P23931; identified by sequence similarity; putativesimilar to GB:X74863, SP:P52954, PID:1617116, and PID:510998; identified by sequence similarity; putative

similar to GP:639829, and GP:639829; identified by sequence similarity; putative

Page 126: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

similar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3603316, and GP:9800449; identified by sequence similarity; putative

similar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3228545, GB:U09067, PID:483876, and PID:553456; identified by sequence similarity; putative

similar to GP:3603319, and GP:3228546; identified by sequence similarity; putativesimilar to GP:3228547, GB:M96789, SP:P35212, and PID:183223; identified by sequence similarity; putative

similar to GP:3603321, and GP:3603255; identified by sequence similarity; putativesimilar to GP:3603256, and GP:3228549; identified by sequence similarity; putative

similar to GP:11276516; identified by sequence similarity; putativesimilar to GP:11276515, and GP:11276515; identified by sequence similarity; putativesimilar to GP:3282779, and GP:11276514; identified by sequence similarity; putative

similar to GP:11276513, GB:L22846, SP:Q14209, and PID:410207; identified by sequence similarity; putativesimilar to GP:3282777, and GP:11276512; identified by sequence similarity; putative

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putativesimilar to GP:11276510; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putative

similar to GP:5360281, and SP:P37929; identified by sequence similarity; putativesimilar to GP:8037778, and GP:8037778; identified by sequence similarity; putative

Also known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putativeidentified by Glimmer2; putative

similar to GP:15980288; identified by sequence similarity; putative

methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNAessential enzyme that recycles AMP in active cells; converts ATP and AMP to two molecules of ADP

adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesisBinds with the catalytic core of RNA polymerase to produce the holoenzyme

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)identified by Glimmer2; putative

catalyzes the formation of adenosylcob(III)yrinic acid a,c-diamide from cob(I)yrinic acid a,c-diamide

similar to GP:9946943; identified by sequence similarity; putativeCatalyzes the formation of (d)CDP from ATP and (d)CMP

putative metalloproteasesimilar to SP:P95745; identified by sequence similarity; putativesimilar to SP:P15993; identified by sequence similarity; putative

catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxideidentified by match to TIGR protein family HMM TIGR01449

identified by Glimmer2; putative

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratesPresumed to be involved in the biosynthesis of pyoverdine due to proximity to the rest of the pyoverdine biosynthetic gene cluster. Possibly acts to release the pyoverdine chromophore precursor from PvsA.; similar to GP:9948471; identified by sequence similarity; putative

similar to GP:15159638; identified by sequence similarity; putative

similar to SP:P31304; identified by sequence similarity; putativeidentified by Glimmer2; putative

identified by match to PFAM protein family HMM PF03929Present adjacent to pyoverdine biosynthetic genes; similar to GP:1890776; identified by sequence similarity; putative

This synthetase is the third module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734

Page 127: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P42512, GB:L17325, and PID:306323; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03781

similar to GP:13506638; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF02776

similar to GP:9947544, and SP:P10446; identified by sequence similarity; putativesimilar to SP:P10445, GB:X62643, SP:P39479, and PID:46682; identified by sequence similarity; putative

part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane componentsmolecular chaperone

catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to 2,3-decenoyl-ACP or 3,4-decenoyl-ACP

catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphatecatalyzes the reduction of 3 -phosphoadenylyl sulfate into sulfite

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratesInvolved in nucleic acid metabolism

similar to SP:P00437, GB:M30496, SP:P15374, and PID:340074; identified by sequence similarity; putativesimilar to GP:10442739, and SP:P00436; identified by sequence similarity; putative

Binds to the 30S ribosomal subunit and enhances its availability for the initiation of protein synthesis

This protein binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunitidentified by Glimmer2; putative

Activates salicylate by adenylation and transfers the salicylyl moiety to irp2, the non-ribosomal peptide synthetase component of yersiniabactin synthetase. Yersiniabactin is a siderophore.; similar to SP:P40871, GP:2765198, GB:X68560, SP:Q02447, PID:338303, and PID:38418; identified by sequence similarity; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putative

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon; similar to GP:11493181; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon.; similar to GP:11493180; identified by sequence similarity; putative

Presumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putative

previously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putativesimilar to GP:15140237, and SP:P25526; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF04020identified by match to PFAM protein family HMM PF02782

similar to GP:2293414; identified by sequence similarity; putativeCatalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA

can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5 -phosphatessimilar to SP:P37901, SP:P14250, and PID:148571; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF02843identified by Glimmer2; putative

similar to GP:9949964; identified by sequence similarity; putativesimilar to GP:17427046; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR01783

similar to GP:13926036; identified by sequence similarity; putativealso known as AvrPtoB; similar to GP:5702216, and GP:18535643; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR00338

catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconateidentified by Glimmer2; putative

similar to GP:15075777; identified by sequence similarity; putativesimilar to SP:P06128; identified by sequence similarity; putative

similar to SP:P32140, and SP:P32140; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR00034similar to GP:2981048, and SP:P00089; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR01804similar to SP:P06967; identified by sequence similarity; putative

Page 128: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by Glimmer2; putative

Stimulates the activities of the other two initiation factors, IF-2 and IF-3

Catalyzes the first step in the glyoxalate cycle, which converts lipids to carbohydratesProduces ATP from ADP in the presence of a proton gradient across the membrane. Rotates with gamma and delta subunits in a cylinder formed of alternating alpha and beta subunits

identified by match to TIGR protein family HMM TIGR01783similar to SP:P42418; identified by sequence similarity; putativesimilar to SP:P42415; identified by sequence similarity; putative

similar to GP:5881935; identified by sequence similarity; putative

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanineidentified by match to PFAM protein family HMM PF00903

identified by match to TIGR protein family HMM TIGR01783similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF04261identified by match to PFAM protein family HMM PF04302

identified by match to TIGR protein family HMM TIGR01293similar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Catalyzes the carboxylation of acetyl-CoA to malonyl-CoACatalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP

identified by Glimmer2; putativeidentified by match to PFAM protein family HMM PF00903

similar to GP:3089521, and GP:3089521; identified by sequence similarity; putative3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphate

forms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolAsimilar to GP:5514778, and SP:P50600; identified by sequence similarity; putativesimilar to SP:P32722, and SP:P32722; identified by sequence similarity; putative

catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAspreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putative

similar to SP:P04816, and SP:P21175; identified by sequence similarity; putative

similar to GP:13625473, and SP:P80415; identified by sequence similarity; putativesimilar to GP:4378826, and SP:P13655; identified by sequence similarity; putativesimilar to SP:P22759, and SP:P22759; identified by sequence similarity; putative

Converts glycerol and ADP to glycerol-3-phosphate and ADP

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to GP:11128402; identified by sequence similarity; putativesimilar to GP:11128403; identified by sequence similarity; putative

similar to GP:11128404, and GP:11128404; identified by sequence similarity; putativesimilar to SP:P06758; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:12620626, and GP:12620626; identified by sequence similarity; putative

similar to GP:7799213; identified by sequence similarity; putativesimilar to SP:P00923; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF00724similar to SP:P53641; identified by sequence similarity; putative

Page 129: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesissimilar to GP:9950620; identified by sequence similarity; putative

Catalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesissimilar to SP:P25663, GB:S50157, GB:X60221, SP:P24539, and PID:509291; identified by sequence similarity; putative

similar to GP:4336803; identified by sequence similarity; putativesimilar to GP:4336801, and GP:4336801; identified by sequence similarity; putative

identified by match to TIGR protein family HMM TIGR01186similar to GP:4138364, and GP:4138364; identified by sequence similarity; putative

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes

Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate

catalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis

identified by match to PFAM protein family HMM PF00141similar to SP:P23847; identified by sequence similarity; putativesimilar to SP:P23847; identified by sequence similarity; putative

similar to GP:9950741, and SP:P32722; identified by sequence similarity; putative

identified by Glimmer2; putative

identified by Glimmer2; putativePreviously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).

identified by Glimmer2; putativePreviously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

identified by Glimmer2; putativesimilar to GP:15075123, and GP:13926142; identified by sequence similarity; putative

similar to GP:15082090; identified by sequence similarity; putativeidentified by Glimmer2; putative

Possibly the ligase which activates coronafacic acid and transfers it to CoA or an acyl carrier protein.; similar to GP:7649554, and PIR:PC4426; identified by sequence similarity; putativeThis gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putative

This gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativeThis thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putative

Previously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918previously known as HopPtoAA (PMID 11872842; Guttman et al, 2002)

previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987identified by Glimmer2; putativeidentified by Glimmer2; putative

Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:6472620; identified by sequence similarity; putative

similar to SP:P35076, GB:X64876, and PID:580818; identified by sequence similarity; putativeThe C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putative

previously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putative

binds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21Catalyzes the forst step in the biosynthesis of 2-methylthio-N6-(delta(2)-isopentyl)-adenosine adjacent to the anticodon of several tRNA species

Catalyzes the decarboxylation of phosphatidyl-L-serine to phosphatidylethanoleaminesimilar to GP:9951239; identified by sequence similarity; putative

similar to SP:P24562, and SP:P24562; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01110

heat shock protein involved in degradation of misfolded proteins

catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribolsyl)-ATP in histidine biosynthesis

Page 130: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by match to PFAM protein family HMM PF02987similar to GP:8037768, and GP:8037768; identified by sequence similarity; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putativeidentified by Glimmer2; putative

similar to GP:12544544, and GP:15159386; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03746

identified by Glimmer2; putativesimilar to GP:2290992; identified by sequence similarity; putative

similar to GB:X74143, SP:P55316, PID:516383, and PID:967048; identified by sequence similarity; putativesimilar to GP:15156635; identified by sequence similarity; putative

identified by Glimmer2; putativeidentified by Glimmer2; putative

identified by Glimmer2; putativeidentified by Glimmer2; putative

protein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substratesIdentified by sequence similarity; similar to NC_007005:4533416..4533538, NC_005773:1684970..1685092

Identified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

similar to GP:6273613; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00991

This gene assignment is based in part on its location adjacent to a Tn3 family transposase.; similar to SP:P30739; identified by sequence similarity; putativeAlso known as AvrPphE; similar to GP:571514; identified by sequence similarity; putative

identified by Glimmer2; putativePreviously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putative

Previously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putativesimilar to GP:8572766; identified by sequence similarity; putative

identified by match to PFAM protein family HMM PF03132identified by match to PFAM protein family HMM PF01839

identified by Glimmer2; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putative

Page 131: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

previously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putativePreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putative

similar to SP:P23929, GB:M16447, GB:X04882, SP:P09417, PID:181553, and PID:30819; identified by sequence similarity; putative

similar to SP:Q46851, GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586Catalyzes the conversion of 1-(2-carboxyphenylamino)1-deoxy-D-ribulose 5 phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate during the biopsynthesis of tryptophan

Important for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s

Mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance

located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosome

Page 132: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

Also known as ORF24 (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to TIGR protein family HMM TIGR01449

previously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putative

similar to GP:5919222, GB:M13699, GB:D00025, GB:X69706, GB:M13536, GB:X04136, GB:X04137, GB:X04138, SP:P00450, PID:1335036, PID:1335037, PID:1666064, and PID:180249; identified by sequence similarity; putative

Also known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putative

Previously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

catalyzes the formation of pyruvate and glyoxylate from 4-hydroxy-2-oxoglutarate; or pyruvate and D-glyceraldehyde 3-phosphate from 2-dehydro-3-deoxy-D-glyconate 6-phosphate

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

Page 133: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

similar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putative

Also known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesis

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratesPresumed to be involved in the biosynthesis of pyoverdine due to proximity to the rest of the pyoverdine biosynthetic gene cluster. Possibly acts to release the pyoverdine chromophore precursor from PvsA.; similar to GP:9948471; identified by sequence similarity; putative

Present adjacent to pyoverdine biosynthetic genes; similar to GP:1890776; identified by sequence similarity; putativeThis synthetase is the third module (of five) in the biosynthesis of the P. syringae pyoverdine peptide which is subsequently modified by various enzymes to produce the mature pyoverdine siderophore.; identified by match to TIGR protein family HMM TIGR01734

Page 134: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components

catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

This protein binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit

Activates salicylate by adenylation and transfers the salicylyl moiety to irp2, the non-ribosomal peptide synthetase component of yersiniabactin synthetase. Yersiniabactin is a siderophore.; similar to SP:P40871, GP:2765198, GB:X68560, SP:Q02447, PID:338303, and PID:38418; identified by sequence similarity; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putative

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon; similar to GP:11493181; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence in yersiniabactin biosynthesis operon.; similar to GP:11493180; identified by sequence similarity; putative

Presumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putative

previously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putative

can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5 -phosphates

Page 135: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Produces ATP from ADP in the presence of a proton gradient across the membrane. Rotates with gamma and delta subunits in a cylinder formed of alternating alpha and beta subunits

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

similar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP

3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphateforms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolA

catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAspreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putative

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).

Page 136: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesissimilar to SP:P25663, GB:S50157, GB:X60221, SP:P24539, and PID:509291; identified by sequence similarity; putative

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes

Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate

catalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis

Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

Possibly the ligase which activates coronafacic acid and transfers it to CoA or an acyl carrier protein.; similar to GP:7649554, and PIR:PC4426; identified by sequence similarity; putativeThis gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putative

This gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativeThis thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putative

Previously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918

previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987

Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).

The C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putativepreviously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putative

Catalyzes the forst step in the biosynthesis of 2-methylthio-N6-(delta(2)-isopentyl)-adenosine adjacent to the anticodon of several tRNA species

Page 137: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

protein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substrates

Identified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

This gene assignment is based in part on its location adjacent to a Tn3 family transposase.; similar to SP:P30739; identified by sequence similarity; putative

Previously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 138: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 139: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

Page 140: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 141: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 142: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

similar to SP:P24186, GB:J02685, GB:J03603, GB:M31551, GB:M31547, GB:M31548, GB:M31549, GB:M31550, SP:P05120, PID:1567409, PID:189545, PID:189547, PID:189561, PID:189563, PID:340154, PID:35268, PID:386995, PID:641357, PID:641359, PID:641361, and PID:641374; identified by sequence similarity; putative

Page 143: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

This thioesterase is likely responsible for the release of the coronatine intermediate, CPE (coronatine cyclopentenone) the proposed product of Cfa6. Its biological role may be as an editing function to release abnormal substrates from Cfa6. See Jiralerspong, S. et. al. (2001), Gene 270:191.; similar to GP:4582977, and GP:3114702; identified by sequence similarity; putative

Page 144: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 145: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

Page 146: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 147: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 148: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

locus_tag replicon a/b- a/c- a/b+ a/c+ b-/c- b-/b+PSPTO0022 NC_004578.1 NA NA NA -0.935258 NA NAPSPTO0044 NC_004578.1 NA NA NA -1.25709 NA NAPSPTO0061 NC_004578.1 NA NA NA -1.564984 NA NAPSPTO0062 NC_004578.1 -5.932367 NA -6.215231 NA NA NAPSPTO0067 NC_004578.1 NA NA 3.8413599 3.909999 NA NAPSPTO0068 NC_004578.1 NA NA 4.6545684 4.6928295 NA NAPSPTO0069 NC_004578.1 NA NA 7.1372996 6.9590005 NA NAPSPTO0211 NC_004578.1 NA NA NA 0.9724669 NA NAPSPTO0219 NC_004578.1 NA NA NA 0.8202102 NA NAPSPTO0220 NC_004578.1 NA 0.6441649 NA 0.7811363 NA NAPSPTO0231 NC_004578.1 NA NA NA -0.807538 NA NAPSPTO0283 NC_004578.1 NA 3.7569243 NA 2.3385575 NA NAPSPTO0314 NC_004578.1 NA NA 3.8027727 2.4570779 NA NAPSPTO0371 NC_004578.1 NA NA NA -0.733964 NA NAPSPTO0503 NC_004578.1 NA NA NA -1.814398 NA NAPSPTO0547 NC_004578.1 NA NA NA -0.889579 NA NAPSPTO0549 NC_004578.1 NA NA NA 0.7144517 NA NAPSPTO0552 NC_004578.1 NA NA NA 0.654005 NA NAPSPTO0569 NC_004578.1 NA NA NA -1.397638 NA NAPSPTO0570 NC_004578.1 NA NA NA -1.46596 NA NAPSPTO0588 NC_004578.1 NA NA NA -1.015811 NA NAPSPTO0589 NC_004578.1 NA NA NA -1.19607 NA NAPSPTO0603 NC_004578.1 NA NA NA NA NA NAPSPTO0615 NC_004578.1 NA NA NA 0.2556747 NA NAPSPTO0621 NC_004578.1 NA NA NA 0.2456952 NA NAPSPTO0637 NC_004578.1 NA NA NA 0.1688892 NA NAPSPTO0638 NC_004578.1 NA NA NA 0.1649339 NA NAPSPTO0647 NC_004578.1 NA NA NA 0.2158567 NA NAPSPTO0648 NC_004578.1 NA NA NA 0.2412944 NA NAPSPTO0651 NC_004578.1 NA NA NA 0.234987 NA NAPSPTO0653 NC_004578.1 NA NA -3.539556 -3.450337 NA NAPSPTO0679 NC_004578.1 NA NA NA -2.302015 NA NAPSPTO0703 NC_004578.1 NA NA NA -0.651079 NA NAPSPTO0728 NC_004578.1 NA NA NA -0.603822 NA NAPSPTO0763 NC_004578.1 NA NA NA 0.5935469 NA NAPSPTO0776 NC_004578.1 NA NA NA -1.135762 NA NAPSPTO0834 NC_004578.1 NA NA -1.093207 NA NA NAPSPTO0835 NC_004578.1 NA NA NA -0.827544 NA NAPSPTO0838 NC_004578.1 NA NA NA -1.297307 NA NAPSPTO0851 NC_004578.1 NA NA NA -1.783988 NA NAPSPTO0852 NC_004578.1 NA NA NA -2.186135 NA NAPSPTO5621 NC_004578.1 NA NA NA -1.50138 NA NAPSPTO0853 NC_004578.1 NA NA NA -0.813887 NA NAPSPTO0874 NC_004578.1 NA NA NA -1.270933 NA NAPSPTO0875 NC_004578.1 NA NA NA -2.925747 NA NAPSPTO0876 NC_004578.1 NA NA NA -1.101544 NA NAPSPTO0877 NC_004578.1 NA NA NA -1.954385 NA NAPSPTO0883 NC_004578.1 NA NA NA -1.916402 NA NAPSPTO0954 NC_004578.1 NA NA NA -0.701972 NA NAPSPTO0955 NC_004578.1 NA NA NA -1.053288 NA NAPSPTO0994 NC_004578.1 NA NA NA -0.5896 NA NAPSPTO1102 NC_004578.1 NA 1.0986236 NA NA NA NAPSPTO1213 NC_004578.1 NA NA NA -0.615016 NA NAPSPTO1214 NC_004578.1 NA -2.95335 NA -2.559413 NA NAPSPTO1288 NC_004578.1 NA NA NA -1.508038 NA NAPSPTO1289 NC_004578.1 NA NA NA -1.020779 NA NA

Supplemental Table 3: Differentially regulated genes identified at a p value less than or equal to 0.002 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 149: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO1290 NC_004578.1 NA NA NA -0.442841 NA NAPSPTO1300 NC_004578.1 NA NA NA -0.357844 NA NAPSPTO1301 NC_004578.1 NA NA NA -0.457383 NA NAPSPTO1304 NC_004578.1 NA NA -1.529705 NA NA NAPSPTO1369 NC_004578.1 NA NA NA -1.132222 NA NAPSPTO1370 NC_004578.1 NA NA NA -2.185717 NA NAPSPTO1371 NC_004578.1 NA NA NA -2.250218 NA NAPSPTO1372 NC_004578.1 NA NA NA -2.553906 NA NAPSPTO1373 NC_004578.1 NA NA NA -0.947331 NA NAPSPTO1374 NC_004578.1 NA NA -1.315215 -1.805831 NA NAPSPTO1375 NC_004578.1 NA NA NA -2.787776 NA NAPSPTO1377 NC_004578.1 NA NA NA -1.229379 NA NAPSPTO1378 NC_004578.1 NA NA NA -2.09983 NA NAPSPTO1379 NC_004578.1 NA NA NA -1.531823 NA NAPSPTO1382 NC_004578.1 NA NA NA -0.546063 NA NAPSPTO1383 NC_004578.1 NA NA NA -0.910963 NA NAPSPTO1384 NC_004578.1 NA NA NA -0.882134 NA NAPSPTO1385 NC_004578.1 NA NA NA -1.21181 NA NAPSPTO1386 NC_004578.1 NA NA NA -2.402792 NA NAPSPTO1387 NC_004578.1 NA NA NA -0.878598 NA NAPSPTO1388 NC_004578.1 NA NA NA -0.880623 NA NAPSPTO1389 NC_004578.1 NA NA NA -1.248336 NA NAPSPTO1390 NC_004578.1 NA NA -0.830914 -1.152631 NA -0.888026PSPTO1391 NC_004578.1 NA NA -0.892835 -1.251592 NA -1.119342PSPTO1395 NC_004578.1 NA NA -0.875173 -1.661899 NA NAPSPTO1396 NC_004578.1 NA NA -1.031415 -1.635579 NA NAPSPTO1397 NC_004578.1 NA NA NA -2.095955 NA NAPSPTO1398 NC_004578.1 NA NA NA -1.172721 NA NAPSPTO1399 NC_004578.1 NA NA NA -1.235075 NA NAPSPTO1400 NC_004578.1 NA NA -2.311183 -3.49863 NA NAPSPTO1401 NC_004578.1 NA NA NA -2.321517 NA NAPSPTO1402 NC_004578.1 NA NA -1.106257 -1.733231 NA NAPSPTO1403 NC_004578.1 NA NA NA -2.13161 NA NAPSPTO1404 NC_004578.1 NA NA NA -1.23282 NA NAPSPTO1405 NC_004578.1 NA NA -0.698289 -1.063583 NA NAPSPTO1406 NC_004578.1 NA NA NA -1.546165 NA NAPSPTO5622 NC_004578.1 NA NA NA -0.47389 NA NAPSPTO1408 NC_004578.1 NA NA NA NA NA NAPSPTO1409 NC_004578.1 NA NA NA NA NA NAPSPTO1456 NC_004578.1 NA NA NA 0.4885487 NA NAPSPTO1475 NC_004578.1 NA NA NA 0.684324 NA NAPSPTO1509 NC_004578.1 NA NA NA NA NA NAPSPTO1543 NC_004578.1 NA NA NA 0.4075718 NA NAPSPTO1568 NC_004578.1 NA NA -2.54482 -2.88323 NA NAPSPTO1609 NC_004578.1 NA NA NA -0.968524 NA NAPSPTO1721 NC_004578.1 NA NA NA -0.618334 NA NAPSPTO1724 NC_004578.1 NA NA NA -1.297375 NA NAPSPTO1817 NC_004578.1 NA NA NA -0.882354 NA NAPSPTO2099 NC_004578.1 NA NA NA 0.6865337 NA NAPSPTO2128 NC_004578.1 NA NA NA -2.240612 NA NAPSPTO2130 NC_004578.1 NA NA NA -1.516483 NA NAPSPTO2133 NC_004578.1 NA NA NA NA NA NAPSPTO2137 NC_004578.1 NA NA NA NA NA NAPSPTO2142 NC_004578.1 NA NA NA NA NA NAPSPTO2152 NC_004578.1 NA NA NA 7.3720056 NA NAPSPTO2298 NC_004578.1 NA NA NA 0.4531196 NA NAPSPTO2339 NC_004578.1 NA NA NA NA NA NAPSPTO2379 NC_004578.1 NA NA NA 0.3586306 NA NA

Page 150: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO2589 NC_004578.1 NA NA NA -2.080509 NA NAPSPTO2598 NC_004578.1 NA NA NA NA NA NAPSPTO2600 NC_004578.1 NA NA NA NA NA NAPSPTO2601 NC_004578.1 NA NA NA NA NA NAPSPTO2602 NC_004578.1 NA NA NA NA NA NAPSPTO2605 NC_004578.1 NA NA NA NA NA NAPSPTO2678 NC_004578.1 NA NA NA -1.923894 NA NAPSPTO2719 NC_004578.1 NA NA NA -0.759138 NA NAPSPTO2752 NC_004578.1 NA NA NA NA NA NAPSPTO2853 NC_004578.1 NA NA NA -3.52925 NA NAPSPTO3039 NC_004578.1 NA NA NA -0.537048 NA NAPSPTO3087 NC_004578.1 NA NA NA -0.957291 NA NAPSPTO3120 NC_004578.1 NA NA 2.4163744 1.7678175 NA NAPSPTO3121 NC_004578.1 NA NA NA 1.4718353 NA NAPSPTO3122 NC_004578.1 NA NA 1.5228517 1.6000405 NA NAPSPTO3157 NC_004578.1 NA NA NA NA NA NAPSPTO3282 NC_004578.1 NA NA NA -0.707854 NA NAPSPTO3294 NC_004578.1 NA NA NA 4.9833611 NA NAPSPTO3337 NC_004578.1 NA NA NA NA NA NAPSPTO3352 NC_004578.1 NA 1.409974 NA NA NA NAPSPTO3353 NC_004578.1 NA NA NA -0.389868 NA NAPSPTO3380 NC_004578.1 NA NA NA -1.28414 NA NAPSPTO3381 NC_004578.1 NA NA NA -1.897646 NA NAPSPTO3382 NC_004578.1 NA NA NA NA NA NAPSPTO3455 NC_004578.1 NA NA NA -1.009889 NA NAPSPTO3544 NC_004578.1 NA NA NA -0.992358 NA NAPSPTO3550 NC_004578.1 NA NA NA -0.716147 NA NAPSPTO3551 NC_004578.1 NA NA NA NA NA NAPSPTO3574 NC_004578.1 NA NA 5.0776797 4.8034906 NA NAPSPTO3582 NC_004578.1 NA NA NA -2.726119 NA NAPSPTO3598 NC_004578.1 NA NA 4.7406768 4.8797721 NA NAPSPTO3599 NC_004578.1 NA NA 4.4080581 4.9908334 NA NAPSPTO3700 NC_004578.1 NA NA -0.803881 NA NA NAPSPTO3836 NC_004578.1 NA 0.9193201 NA 0.6709119 NA NAPSPTO3925 NC_004578.1 NA NA NA -0.935669 NA NAPSPTO3959 NC_004578.1 NA NA NA -0.729666 NA NAPSPTO4101 NC_004578.1 NA NA NA -1.258466 NA NAPSPTO4145 NC_004578.1 NA NA NA 0.863006 NA NAPSPTO4159 NC_004578.1 NA NA 6.426395 7.471834 NA NAPSPTO4160 NC_004578.1 NA NA -4.271013 -4.379085 NA NAPSPTO4168 NC_004578.1 NA NA NA -0.716317 NA NAPSPTO4174 NC_004578.1 NA NA NA -0.451413 NA NAPSPTO4232 NC_004578.1 NA NA -4.283955 NA NA NAPSPTO4233 NC_004578.1 NA NA -3.148023 NA NA NAPSPTO4234 NC_004578.1 NA NA -2.234802 NA NA NAPSPTO4285 NC_004578.1 NA NA NA -2.361196 NA NAPSPTO4297 NC_004578.1 NA NA NA -1.894108 NA NAPSPTO4331 NC_004578.1 NA NA NA -0.575976 NA NAPSPTO4332 NC_004578.1 NA NA NA NA NA NAPSPTO4333 NC_004578.1 NA NA NA -1.630766 NA NAPSPTO4358 NC_004578.1 NA NA NA -0.496201 NA NAPSPTO4366 NC_004578.1 NA NA 5.6377242 2.2418911 NA NAPSPTO4367 NC_004578.1 NA NA 2.994826 2.2354584 NA NAPSPTO4368 NC_004578.1 NA NA 2.57355 NA NA NAPSPTO4369 NC_004578.1 NA NA 1.6313637 0.8441955 NA NAPSPTO4381 NC_004578.1 NA NA 1.8012265 2.1540737 NA NAPSPTO4442 NC_004578.1 NA 1.397263 NA NA NA NAPSPTO4456 NC_004578.1 NA NA NA 0.8525176 NA NA

Page 151: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4507 NC_004578.1 NA NA NA -0.897708 NA NAPSPTO4530 NC_004578.1 NA NA NA -0.707174 NA NAPSPTO4558 NC_004578.1 NA NA 0.7495851 NA NA NAPSPTO4578 NC_004578.1 NA NA NA 1.6063946 NA NAPSPTO4588 NC_004578.1 NA NA NA -2.085412 NA NAPSPTO4589 NC_004578.1 NA NA NA -1.580561 NA NAPSPTO4597 NC_004578.1 NA NA NA -1.8858 NA NAPSPTO4599 NC_004578.1 NA NA NA -1.418736 NA NAPSPTO4647 NC_004578.1 NA NA NA -3.151012 NA NAPSPTO4686 NC_004578.1 NA NA NA -0.328762 NA NAPSPTO4687 NC_004578.1 NA NA NA -0.411068 NA NAPSPTO4691 NC_004578.1 NA NA NA -2.28565 NA NAPSPTO4704 NC_004578.1 NA NA NA -1.312865 NA NAPSPTO4718 NC_004578.1 NA NA NA -1.992004 NA NAPSPTO4720 NC_004578.1 NA NA NA -0.507764 NA NAPSPTO4721 NC_004578.1 NA NA NA -0.530916 NA NAPSPTO4727 NC_004578.1 NA NA NA -3.526454 NA NAPSPTO4733 NC_004578.1 NA NA NA -1.930883 NA NAPSPTO4766 NC_004578.1 NA NA NA -1.070108 NA NAPSPTO4776 NC_004578.1 NA NA NA NA NA NAPSPTO4933 NC_004578.1 NA NA NA 0.2722594 NA NAPSPTO5255 NC_004578.1 NA NA NA -0.761021 NA NAPSPTO5256 NC_004578.1 NA NA NA -1.578395 NA NAPSPTO5353 NC_004578.1 NA NA NA NA NA NAPSPTO5354 NC_004578.1 NA NA NA -1.151489 NA NAPSPTO5377 NC_004578.1 NA NA NA 2.8623793 NA NAPSPTO5378 NC_004578.1 NA 3.8950923 NA 3.2728285 NA NAPSPTO5379 NC_004578.1 NA 2.5138799 NA 1.6877617 NA NAPSPTO5380 NC_004578.1 NA 3.2082837 NA 2.8727084 NA NAPSPTO5381 NC_004578.1 NA 3.7296646 NA 3.0217049 NA NAPSPTO5474 NC_004578.1 NA NA NA NA NA NAPSPTO5517 NC_004578.1 NA NA NA -0.759383 NA NAPSPTO5614 NC_004578.1 NA NA NA 0.5010452 NA NAPSPTO_B0005 NC_004632.1 NA NA NA -0.896596 NA NAPSPTO_B0012 NC_004632.1 NA NA NA NA NA NAPSPTO_B0026 NC_004632.1 NA NA NA -0.777345 NA NAPSPTOA0008 NC_004633.1 NA NA NA -0.660665 NA NAPSPTOA0012 NC_004633.1 NA NA NA -1.373186 NA NAPSPTOA0017 NC_004633.1 NA NA NA -0.898187 NA NAPSPTOA0018 NC_004633.1 NA NA NA -0.885862 NA NAPSPTOA0019 NC_004633.1 NA NA NA -1.21726 NA NA

NC_004578.1 NA NA 7.7506725 NA NA NAsmall RNA prrF2

Page 152: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

c-/c+ b+/c+ nameNA NANA NA hopK1-1.837164 NA hopY1

NA 4.62060065.2431938 NA tonB-16.4724107 NA exbD-18.8815456 NA exbB-1NA NA iucDNA NANA NANA -0.969471NA NA3.2081509 NANA NA iaaL-2.096007 NA shcF

NA NANA NA apaHNA NA pdxANA -1.563118NA NA-1.522258 NA hopH1-1.330995 NA hopC1-1.333644 NA

NA NA rplKNA NA rpsLNA NA rplXNA NA rplENA NA rpmJNA NA rpsMNA NA rpoANA NANA NANA NANA NANA NA fecBNA NA recCNA NANA NANA NA-2.631302 NA-1.869806 NA hopAJ1

NA NANA NANA NA

-3.60018 NA-1.136097 NA hopD1-1.889711 NA hopQ1-1-1.250294 NA hopR1

NA -0.712299NA NA fruKNA NANA NA pthNA NANA NANA NA eddNA NA glk

: Differentially regulated genes identified at a p value less than or equal to 0.002 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 153: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NANA NA zwf-1NA -0.584589 pglNA NA-1.316473 NA-2.227402 NA hopN1

NA NA-2.561653 NA hopAA1-1

NA NA hrpW1-2.115172 NA shcM-2.822233 NA hopM1

NA NA avrE1-2.406927 NA-2.414211 NA hrpR

NA NA hrpZ1NA NA hrpB(Pto)-1.311128 NA hrcJ-1.611665 NA hrpD-2.790877 NA hrpE-1.620227 NA hrpF-1.393513 NA hrpG-1.425796 NA hrcC

-1.321 NA hrpT-1.779791 NA hrpV-1.751173 NA hrcR-1.888265 NA hrcQb-2.364174 NA hrcQa-1.652615 NA hrpP-1.735737 NA hrpO-4.469206 NA hrcN-2.537096 NA hrpQ-2.053826 NA hrcV-2.508559 NA hrpJ-1.729669 NA hrpL

NA NA hrpK1NA NA hopB1NA NA-2.976955 NA-2.312568 NA

NA NA cumANA NA trmD-0.531011 NA adk

NA NA-4.379087 NA hopAF1-0.761407 NA

NA NANA NANA NANA NANA NA-1.571067 NA8.6313434 NA9.0235798 NA4.4037076 NA11.478055 NANA NA-1.724496 NA pcaG

NA NA infC

Page 154: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA9.2882023 NA irp4

10.3148 NA irp19.8562613 NA10.275206 NA9.3737924 NANA NA hopP1NA NANA -0.551873 tpxNA NANA NA-1.072279 NA hopAB2

NA NA1.9114979 NA zwf-22.0177668 NA gnd7.3413133 NANA NA6.0026651 NA

-1.19748 NANA NA infANA NA clpA-1.707997 NA-2.138914 NA-1.220539 NA

NA NANA NANA NA fahANA -0.717647 hmgA6.0741522 NA-3.149391 NA katB5.9791688 NA

6.006367 NANA NANA NANA NANA NA nadA-1.202933 NA hopAK1

NA NA capB8.6726328 NANA NA bfrNA NA glpKNA NANA NANA NANA 2.3846269NA NA adhBNA -1.902474-0.778112 NA hopE1-2.257178 NA-1.637949 NA

NA NA2.8906637 NANA NANA NANA NANA NANA NANA NA

Page 155: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NA recNNA NA katGNA NANA NA

-1.97661 NA hopS2-1.421445 NA shcS2-3.303099 NA hopS1-1.609763 NA shcS1

NA NA cioBNA NA cfa6NA NA cfa7NA NA hopAD1NA NA corR

-2.01319 NA hopAA1-2NA NA hopV1NA NA shcVNA NA hopG1-2.561408 NA

NA NA-1.05818 NA hopI1

NA NA rpsFNA NA cynT-1.347329 NA-2.579072 NA shcA-1.565909 NA hopA1

NA NANA 3.0034822NA NANA NANA NA-0.957503 NA rubA

NA NANA NA rnpA-0.974053 NA plcA2-1.157763 NA

NA NANA NA-1.478059 NA HopX1-1.306641 NA shc01-0.881881 NA hopO1-1

-1.70248 NA hopT1-1NA NA prrF2

Page 156: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

annotationDNA-binding proteintype III effector HopK1type III effector HopY1citrate transportertonB proteinTonB system transport protein ExbDTonB system transport protein ExbBL-lysine 6-monooxygenasehypothetical proteinhypothetical proteinhypothetical proteinhypothetical proteiniron ABC transporter, periplasmic iron-binding proteinindoleacetate-lysine ligasetype III chaperone protein ShcFhypothetical proteindiadenosinetetraphosphatase4-hydroxythreonine-4-phosphate dehydrogenaseautotransporting lipase, GDSL familytranscriptional regulator PrtN, putativetype III effector HopH1type III effector HopC1hypothetical protein50S ribosomal protein L1130S ribosomal protein S1250S ribosomal protein L2450S ribosomal protein L550S ribosomal protein L3630S ribosomal protein S13DNA-directed RNA polymerase alpha subunitbacterioferritinouter membrane protein OmpWglutathione S-transferase family proteinaldehyde dehydrogenase family proteiniron(III) dicitrate transport system, periplasmic iron-binding protein FecBexodeoxyribonuclease V, gamma subunitalcohol dehydrogenase, zinc-containingribD C-terminal domain proteinmajor facilitator family transporterhypothetical proteintype III effector HopAJ1PSPTO5621dnaK suppressor protein, putativenikkomycin biosynthesis domain proteinhypothetical proteintype III effector HopD1type III effector HopQ1-1type III effector HopR1phosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components1-phosphofructokinasecarbonic anhydrasepeptidyl-tRNA hydrolasetranscriptional regulator, AraC familymembrane proteinphosphogluconate dehydrataseglucokinase

: Differentially regulated genes identified at a p value less than or equal to 0.002 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 157: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

DNA-binding response regulatorglucose-6-phosphate 1-dehydrogenase6-phosphogluconolactonasehypothetical proteinconserved effector locus proteintype III effector HopN1conserved effector locus proteintype III effector HopAA1-1type III helper protein HrpW1type III chaperone ShcMtype III effector HopM1type III effector protein AvrE1membrane-bound lytic murein transglycosylase D, putativetype III transcriptional regulator HrpRtype III helper protein HrpZ1type III secretion protein HrpB(Pto)type III secretion protein HrcJtype III secretion protein HrpDtype III secretion protein HrpEtype III secretion protein HrpFtype III secretion protein HrpGouter-membrane type III secretion protein HrcCtype III secretion protein HrpTnegative regulator of hrp expression HrpVtype III secretion protein HrcRtype III secretion protein HrcQbtype III secretion protein HrcQatype III secretion protein HrpPtype III secretion protein HrpOtype III secretion cytoplasmic ATPase HrcNtype III secretion protein HrpQtype III secretion protein HrcVtype III secretion protein HrpJRNA polymerase sigma factor HrpLtype III helper protein HrpK1type III effector HopB1PSPTO5622hypothetical proteinhypothetical proteinmulticopper oxidasetRNA (guanine-N(1)-)-methyltransferaseadenylate kinaseouter membrane protein OmpH, putativetype III effector HopAF1hypothetical proteinhypothetical proteinhypothetical proteinaromatic amino acid permeasehelicase SNF2 family domain proteinresponse regulatorDNA-binding response regulator, LuxR familyRNA polymerase sigma-70 factorMbtH-like proteinhypothetical proteinTonB-dependent siderophore receptor, putativeRNA polymerase sigma-70 factorprotocatechuate 3,4-dioxygenase, alpha subunittranslation initiation factor IF-3

Page 158: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

hypothetical proteinyersiniabactin synthetase, thioesterase componentyersiniabactin polyketide non-ribosomal peptide synthetasehypothetical proteinyersiniabactin non-ribosomal peptide synthetaseTonB-dependent siderophore receptor, putativetype III helper protein HopP1enoyl-CoA hydratasethiol peroxidaseTonB-dependent receptor, putativealcohol dehydrogenase, zinc-containingtype III effector HopAB2Cof-like hydrolase family proteinglucose-6-phosphate 1-dehydrogenase6-phosphogluconate dehydrogenasehypothetical proteinlipoprotein, putativeTonB-dependent siderophore receptor, putativehypothetical proteintranslation initiation factor IF-1ATP-dependent clp protease, ATP-binding subunit ClpAsensor histidine kinaseDNA-binding response regulatorlipoprotein, putative3-oxoacid CoA-transferase, subunit A familyhypothetical proteinfumarylacetoacetasehomogentisate 1,2-dioxygenaseTonB-dependent siderophore receptor, putativecatalasedyp-type peroxidase family proteinhypothetical proteinoxidoreductase, aldo keto reductase familyhypothetical proteingas vesicle protein, putativequinolinate synthetasetype III effector HopAK1cold shock protein CapBbacterioferritin-associated ferredoxinbacterioferritinglycerol kinaseamino acid ABC transporter, ATP-binding proteinTctC protein, putativemembrane protein TctB, putativemembrane protein TctA, putativealcohol dehydrogenase IIhypothetical proteintype III effector HopE1hypothetical proteinmoxR protein, putativeoxidoreductase, FAD FMN-bindingiron-regulated protein A, putativelipoprotein, putativelipoprotein, putativelipoprotein, putativehypothetical proteintoluene tolerance protein, putativehypothetical protein

Page 159: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

DNA repair protein RecNcatalase peroxidase HPIdipeptide ABC transporter, periplasmic dipeptide-binding protein, putativeglycine betaine carnitine choline ABC transporter, permease proteintype III effector HopS2type III chaperone ShcS2type III effector HopS1type III chaperone ShcS1cyanide-insensitive terminal oxidase CioBcoronafacic acid polyketide synthase Icoronafacic acid polyketide synthetase IItype III effector HopAD1DNA-binding response regulator CorRtype III effector HopAA1-2type III effector HopV1type III chaperone ShcVtype III effector HopG1hypothetical proteinhypothetical proteintype III effector HopI130S ribosomal protein S6carbonic anhydrasesulfate transporter family proteintype III chaperone protein ShcAtype III effector HopA1hypothetical proteinhypothetical proteinhypothetical proteinallophanate hydrolase, putativebiotin carboxylase biotin carboxyl carrier proteinrubredoxinhypothetical proteinribonuclease Pphosphoesterase family proteinhypothetical proteinhypothetical proteinpartion protein, ParB familytype III effector HopX1type III chaperone ShcO1type III effector HopO1-1type III effector HopT1-1within intergenic region 3549362-3549773

Page 160: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

notesidentified by match to PFAM protein family HMM PF01381previously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putativePreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to GP:14595286, and GP:14595286; identified by sequence similarity; putativesimilar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putativesimilar to GP:14595284; identified by sequence similarity; putativesimilar to SP:P11295; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00149identified by Glimmer2; putative

identified by Glimmer2; putative

similar to SP:P18204, GB:J04031, SP:P11586, and PID:307178; identified by sequence similarity; putative

similar to SP:P77391; identified by sequence similarity; putativeCatalyzes the hydrolysis of P1,P4-bis(5 -adenosyl) tetraphosphateAn essential cofactor for many enzymes responsible for the metabolic conversions of amino acids

previously known as HopPtoH (PMID 12032338; Petnicki-Ocwieja et al, 2002).previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586

binds directly to 23S ribosomal RNAImportant for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S sFound in the ribonucleoprotein core and is involved in the early assembly of the 50S subunitMediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberanceRibosomal protein L36 is the smallest protein from the large subunit of the prokaryotic ribosomeLocated at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNACatalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

similar to GB:M59829, SP:P34931, SP:P48741, and PID:188492; identified by sequence similarity; putative

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01751similar to GB:S69136, GB:S69198, GB:M28594, and PID:292763; identified by sequence similarity; putativesimilar to GB:U01783, and PID:409855; identified by sequence similarity; putativesimilar to SP:P77262; identified by sequence similarity; putativepreviously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putativeIdentified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.similar to SP:P18274, GB:M25499, SP:P16588, and PID:155251; identified by sequence similarity; putativesimilar to GP:14030855; identified by sequence similarity; putativeAlso known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putativeEnables the recycling of peptidyl-tRNAs produced at termination of translationsimilar to GP:13936369; identified by sequence similarity; putativesimilar to GP:13936368; identified by sequence similarity; putativecatalyzes the formation of 2-dehydro-3-deoxy-6-phospho-D-gluconate from 6-phospho-D-gluconatecatalyzes the conversion of ATP and D-glucose to ADP and D-glucose 6-phosphate

: Differentially regulated genes identified at a p value less than or equal to 0.002 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log 2

Page 161: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphatecatalyzes the formation of 6-phospho-D-gluconate from 6-phospho-D-glucono-1,5-lactone

similar to GP:8037800; identified by sequence similarity; putativeAlso known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586similar to GP:8037798, SP:P32109, GB:U15124, and PID:563996; identified by sequence similarity; putativepreviously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987similar to GP:3694999, and GP:8037796; identified by sequence similarity; putative

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putativesimilar to SP:P23931; identified by sequence similarity; putativesimilar to GB:X74863, SP:P52954, PID:1617116, and PID:510998; identified by sequence similarity; putativesimilar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3603316, and GP:9800449; identified by sequence similarity; putativesimilar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3228545, GB:U09067, PID:483876, and PID:553456; identified by sequence similarity; putativesimilar to GP:3603319, and GP:3228546; identified by sequence similarity; putativesimilar to GP:3228547, GB:M96789, SP:P35212, and PID:183223; identified by sequence similarity; putativesimilar to GP:3603321, and GP:3603255; identified by sequence similarity; putativesimilar to GP:3603256, and GP:3228549; identified by sequence similarity; putativesimilar to GP:11276516; identified by sequence similarity; putativesimilar to GP:11276515, and GP:11276515; identified by sequence similarity; putativesimilar to GP:3282779, and GP:11276514; identified by sequence similarity; putativesimilar to GP:11276513, GB:L22846, SP:Q14209, and PID:410207; identified by sequence similarity; putativesimilar to GP:3282777, and GP:11276512; identified by sequence similarity; putativesimilar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putativesimilar to GP:11276510; identified by sequence similarity; putativesimilar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putativesimilar to GP:5360281, and SP:P37929; identified by sequence similarity; putativesimilar to GP:8037778, and GP:8037778; identified by sequence similarity; putativeAlso known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

identified by Glimmer2; putativesimilar to GP:15980288; identified by sequence similarity; putative

methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNAessential enzyme that recycles AMP in active cells; converts ATP and AMP to two molecules of ADP

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)identified by Glimmer2; putative

similar to GP:9946943; identified by sequence similarity; putativesimilar to SP:P15993; identified by sequence similarity; putative

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to GP:15159638; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to SP:P42512, GB:L17325, and PID:306323; identified by sequence similarity; putativeDNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substratessimilar to GP:10442739, and SP:P00436; identified by sequence similarity; putativeBinds to the 30S ribosomal subunit and enhances its availability for the initiation of protein synthesis

Page 162: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by Glimmer2; putativePossibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putativepreviously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putativeCatalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoAsimilar to SP:P37901, SP:P14250, and PID:148571; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR01783similar to GP:13926036; identified by sequence similarity; putativealso known as AvrPtoB; similar to GP:5702216, and GP:18535643; identified by sequence similarity; putativeidentified by match to TIGR protein family HMM TIGR00338

catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconateidentified by Glimmer2; putative

similar to GP:2981048, and SP:P00089; identified by sequence similarity; putativeidentified by Glimmer2; putativeStimulates the activities of the other two initiation factors, IF-2 and IF-3

similar to GP:5881935; identified by sequence similarity; putative

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanineidentified by match to TIGR protein family HMM TIGR01783similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF04261identified by match to PFAM protein family HMM PF04302identified by match to TIGR protein family HMM TIGR01293identified by Glimmer2; putativesimilar to GP:3089521, and GP:3089521; identified by sequence similarity; putative3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphatepreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putativesimilar to GP:13625473, and SP:P80415; identified by sequence similarity; putativesimilar to GP:4378826, and SP:P13655; identified by sequence similarity; putativesimilar to SP:P22759, and SP:P22759; identified by sequence similarity; putativeConverts glycerol and ADP to glycerol-3-phosphate and ADP

similar to GP:11128402; identified by sequence similarity; putativesimilar to GP:11128403; identified by sequence similarity; putativesimilar to GP:11128404, and GP:11128404; identified by sequence similarity; putativesimilar to SP:P06758; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:12620626, and GP:12620626; identified by sequence similarity; putativesimilar to GP:7799213; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF00724

similar to GP:9950620; identified by sequence similarity; putativesimilar to GP:4336803; identified by sequence similarity; putativesimilar to GP:4138364, and GP:4138364; identified by sequence similarity; putative

Page 163: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

identified by match to PFAM protein family HMM PF00141similar to SP:P23847; identified by sequence similarity; putative

Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).identified by Glimmer2; putativePreviously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putativeidentified by Glimmer2; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativePreviously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918

previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987identified by Glimmer2; putativeidentified by Glimmer2; putativePreviously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:6472620; identified by sequence similarity; putativeThe C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putativepreviously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putativebinds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21

similar to GP:8037768, and GP:8037768; identified by sequence similarity; putativepreviously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putativesimilar to GP:12544544, and GP:15159386; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03746identified by Glimmer2; putativesimilar to GP:2290992; identified by sequence similarity; putativesimilar to GB:X74143, SP:P55316, PID:516383, and PID:967048; identified by sequence similarity; putative

identified by Glimmer2; putativeprotein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substratessimilar to GP:8572766; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF01839identified by Glimmer2; putativesimilar to GP:6273613; identified by sequence similarity; putativeAlso known as AvrPphE; similar to GP:571514; identified by sequence similarity; putativeidentified by Glimmer2; putativePreviously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 164: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

previously known as HopPtoK (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoAB (PMID 11872842; Guttman et al, 2002); similar to GP:1008894; identified by sequence similarity; putativePreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putative

previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586

Important for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s

Mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

previously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putativeIdentified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

Also known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

: Differentially regulated genes identified at a p value less than or equal to 0.002 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log 2.

Page 165: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putative

Also known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates

Page 166: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Possibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeLikely involved in siderophore function due to conserved localization within the yersiniabactin gene cluster.; similar to GP:4106631, and GP:21959254; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putativepreviously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putative

An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphatepreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).

Page 167: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putativePreviously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918

previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987

Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).

The C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putativepreviously known as HopPmaI (PMID 11872842; Guttman et al, 2002); similar to GP:19071496; identified by sequence similarity; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

protein compoenent of RNaseP which catalyzes the removal of the 5 -leader sequence from pre-tRNA to produce the mature 5 terminus; this enzyme also cleaves other RNA substrates

Previously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 168: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Important for translational accuracy. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to GB:M68516, GB:S69366, GB:S69363, GB:S69364, GB:S69574, GB:S69365, GB:J02639, GB:S58545, GB:U35464, SP:P05154, PID:1144561, PID:180550, and PID:189678; identified by sequence similarity; putative

Identified by sequence similarity; similar to NC_005773:895723..895944, complement(NC_007274:90904..91125), complement(NC_007274:61838..62053), complement(NC_007284:5068..5383); N-terminus similar to carbon storage regulator proteins.

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

Page 169: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putative

Page 170: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Possibly involved in the release of an intermediate product similar to pyochelin, since the terminal yersiniabactin synthetase has its own thioesterase domain.; similar to GP:3818607; identified by sequence similarity; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

Page 171: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

Previously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 172: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:X66899, GB:X72990, GB:X72991, GB:X72992, GB:X72993, GB:X72994, GB:X72995, GB:X72996, GB:X72997, GB:X72998, GB:X72999, GB:X73000, GB:X73001, GB:X73002, GB:X73003, GB:X73004, SP:Q01844, PID:1572086, PID:1666068, PID:31280, and PID:825654; identified by sequence similarity; putative

Page 173: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 174: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putative

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

Page 175: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

Page 176: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 177: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 178: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 179: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7).; similar to GP:13346874; identified by sequence similarity; putativeThis gene is the second of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPE (2-[1-oxo-2-cyclopenten-2-ylmethyl]butanoic acid) from the first synthetase, Cpe6. It then adds one final acetate group, catalyzes the cyclization of the second ring and converts a ketone to a double bond. The product is released by a terminal thioesterase domain.; similar to GP:13162634; identified by sequence similarity; putative

Page 180: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 181: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 182: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 183: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 184: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 185: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 186: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

locus_tag replicon a/b- a/c- a/b+ a/c+ b-/c- b-/b+PSPTO0061 NC_004578.1 NA NA NA -1.564984 NA NAPSPTO0062 NC_004578.1 -5.932367 NA -6.215231 NA NA NAPSPTO0067 NC_004578.1 NA NA NA 3.909999 NA NAPSPTO0068 NC_004578.1 NA NA 4.6545684 4.6928295 NA NAPSPTO0069 NC_004578.1 NA NA 7.1372996 6.9590005 NA NAPSPTO0211 NC_004578.1 NA NA NA 0.9724669 NA NAPSPTO0220 NC_004578.1 NA 0.6441649 NA 0.7811363 NA NAPSPTO0283 NC_004578.1 NA NA NA 2.3385575 NA NAPSPTO0314 NC_004578.1 NA NA 3.8027727 2.4570779 NA NAPSPTO0371 NC_004578.1 NA NA NA -0.733964 NA NAPSPTO0503 NC_004578.1 NA NA NA -1.814398 NA NAPSPTO0547 NC_004578.1 NA NA NA -0.889579 NA NAPSPTO0549 NC_004578.1 NA NA NA 0.7144517 NA NAPSPTO0569 NC_004578.1 NA NA NA -1.397638 NA NAPSPTO0570 NC_004578.1 NA NA NA -1.46596 NA NAPSPTO0588 NC_004578.1 NA NA NA -1.015811 NA NAPSPTO0589 NC_004578.1 NA NA NA -1.19607 NA NAPSPTO0637 NC_004578.1 NA NA NA 0.1688892 NA NAPSPTO0638 NC_004578.1 NA NA NA 0.1649339 NA NAPSPTO0647 NC_004578.1 NA NA NA 0.2158567 NA NAPSPTO0653 NC_004578.1 NA NA NA -3.450337 NA NAPSPTO0728 NC_004578.1 NA NA NA -0.603822 NA NAPSPTO0763 NC_004578.1 NA NA NA 0.5935469 NA NAPSPTO0851 NC_004578.1 NA NA NA -1.783988 NA NAPSPTO0852 NC_004578.1 NA NA NA -2.186135 NA NAPSPTO0874 NC_004578.1 NA NA NA -1.270933 NA NAPSPTO0875 NC_004578.1 NA NA NA -2.925747 NA NAPSPTO0876 NC_004578.1 NA NA NA -1.101544 NA NAPSPTO0877 NC_004578.1 NA NA NA -1.954385 NA NAPSPTO0883 NC_004578.1 NA NA NA -1.916402 NA NAPSPTO0954 NC_004578.1 NA NA NA -0.701972 NA NAPSPTO0955 NC_004578.1 NA NA NA -1.053288 NA NAPSPTO1290 NC_004578.1 NA NA NA -0.442841 NA NAPSPTO1301 NC_004578.1 NA NA NA -0.457383 NA NAPSPTO1369 NC_004578.1 NA NA NA -1.132222 NA NAPSPTO1370 NC_004578.1 NA NA NA -2.185717 NA NAPSPTO1371 NC_004578.1 NA NA NA -2.250218 NA NAPSPTO1372 NC_004578.1 NA NA NA -2.553906 NA NAPSPTO1373 NC_004578.1 NA NA NA -0.947331 NA NAPSPTO1374 NC_004578.1 NA NA NA -1.805831 NA NAPSPTO1375 NC_004578.1 NA NA NA -2.787776 NA NAPSPTO1377 NC_004578.1 NA NA NA -1.229379 NA NAPSPTO1378 NC_004578.1 NA NA NA -2.09983 NA NAPSPTO1382 NC_004578.1 NA NA NA -0.546063 NA NAPSPTO1383 NC_004578.1 NA NA NA -0.910963 NA NAPSPTO1384 NC_004578.1 NA NA NA -0.882134 NA NAPSPTO1385 NC_004578.1 NA NA NA -1.21181 NA NAPSPTO1386 NC_004578.1 NA NA NA -2.402792 NA NAPSPTO1387 NC_004578.1 NA NA NA -0.878598 NA NAPSPTO1388 NC_004578.1 NA NA NA NA NA NAPSPTO1389 NC_004578.1 NA NA NA -1.248336 NA NAPSPTO1390 NC_004578.1 NA NA NA -1.152631 NA NAPSPTO1391 NC_004578.1 NA NA NA -1.251592 NA -1.119341PSPTO1395 NC_004578.1 NA NA -0.875173 -1.661899 NA NAPSPTO1396 NC_004578.1 NA NA NA -1.635579 NA NAPSPTO1397 NC_004578.1 NA NA NA -2.095955 NA NA

Supplemental Table 4: Differentially regulated genes identified at a p value less than or equal to 0.0004 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 187: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO1398 NC_004578.1 NA NA NA -1.172721 NA NAPSPTO1399 NC_004578.1 NA NA NA NA NA NAPSPTO1400 NC_004578.1 NA NA -2.311183 -3.49863 NA NAPSPTO1401 NC_004578.1 NA NA NA -2.321517 NA NAPSPTO1402 NC_004578.1 NA NA NA -1.733231 NA NAPSPTO1403 NC_004578.1 NA NA NA -2.13161 NA NAPSPTO1404 NC_004578.1 NA NA NA -1.23282 NA NAPSPTO1405 NC_004578.1 NA NA NA -1.063583 NA NAPSPTO1406 NC_004578.1 NA NA NA -1.546165 NA NAPSPTO1408 NC_004578.1 NA NA NA NA NA NAPSPTO1456 NC_004578.1 NA NA NA 0.4885487 NA NAPSPTO1475 NC_004578.1 NA NA NA 0.684324 NA NAPSPTO1568 NC_004578.1 NA NA -2.54482 -2.88323 NA NAPSPTO1609 NC_004578.1 NA NA NA -0.968524 NA NAPSPTO1817 NC_004578.1 NA NA NA -0.882354 NA NAPSPTO2128 NC_004578.1 NA NA NA -2.240612 NA NAPSPTO2130 NC_004578.1 NA NA NA -1.516483 NA NAPSPTO2137 NC_004578.1 NA NA NA NA NA NAPSPTO2142 NC_004578.1 NA NA NA NA NA NAPSPTO2152 NC_004578.1 NA NA NA NA NA NAPSPTO2339 NC_004578.1 NA NA NA NA NA NAPSPTO2379 NC_004578.1 NA NA NA 0.3586306 NA NAPSPTO2589 NC_004578.1 NA NA NA -2.080509 NA NAPSPTO2600 NC_004578.1 NA NA NA NA NA NAPSPTO2602 NC_004578.1 NA NA NA NA NA NAPSPTO2605 NC_004578.1 NA NA NA NA NA NAPSPTO2678 NC_004578.1 NA NA NA -1.923894 NA NAPSPTO2719 NC_004578.1 NA NA NA -0.759138 NA NAPSPTO2853 NC_004578.1 NA NA NA -3.52925 NA NAPSPTO3087 NC_004578.1 NA NA NA -0.957291 NA NAPSPTO3121 NC_004578.1 NA NA NA 1.4718353 NA NAPSPTO3122 NC_004578.1 NA NA NA 1.6000405 NA NAPSPTO3157 NC_004578.1 NA NA NA NA NA NAPSPTO3294 NC_004578.1 NA NA NA NA NA NAPSPTO3352 NC_004578.1 NA 1.409974 NA NA NA NAPSPTO3353 NC_004578.1 NA NA NA -0.389868 NA NAPSPTO3381 NC_004578.1 NA NA NA -1.897646 NA NAPSPTO3382 NC_004578.1 NA NA NA NA NA NAPSPTO3574 NC_004578.1 NA NA 5.0776797 4.8034906 NA NAPSPTO3582 NC_004578.1 NA NA NA -2.726119 NA NAPSPTO3598 NC_004578.1 NA NA 4.7406768 4.8797721 NA NAPSPTO3599 NC_004578.1 NA NA 4.4080581 4.9908334 NA NAPSPTO3836 NC_004578.1 NA 0.9193201 NA NA NA NAPSPTO3959 NC_004578.1 NA NA NA -0.729666 NA NAPSPTO4101 NC_004578.1 NA NA NA -1.258466 NA NAPSPTO4145 NC_004578.1 NA NA NA 0.863006 NA NAPSPTO4159 NC_004578.1 NA NA 6.426395 7.471834 NA NAPSPTO4160 NC_004578.1 NA NA NA -4.379085 NA NAPSPTO4168 NC_004578.1 NA NA NA -0.716317 NA NAPSPTO4232 NC_004578.1 NA NA -4.283955 NA NA NAPSPTO4233 NC_004578.1 NA NA -3.148023 NA NA NAPSPTO4234 NC_004578.1 NA NA -2.234802 NA NA NAPSPTO4297 NC_004578.1 NA NA NA -1.894108 NA NAPSPTO4331 NC_004578.1 NA NA NA NA NA NAPSPTO4333 NC_004578.1 NA NA NA -1.630766 NA NAPSPTO4366 NC_004578.1 NA NA NA 2.2418911 NA NAPSPTO4367 NC_004578.1 NA NA 2.994826 NA NA NAPSPTO4368 NC_004578.1 NA NA 2.57355 NA NA NA

Page 188: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

PSPTO4369 NC_004578.1 NA NA 1.6313637 NA NA NAPSPTO4381 NC_004578.1 NA NA 1.8012265 2.1540737 NA NAPSPTO4442 NC_004578.1 NA 1.397263 NA NA NA NAPSPTO4588 NC_004578.1 NA NA NA -2.085412 NA NAPSPTO4589 NC_004578.1 NA NA NA -1.580561 NA NAPSPTO4597 NC_004578.1 NA NA NA NA NA NAPSPTO4599 NC_004578.1 NA NA NA -1.418736 NA NAPSPTO4691 NC_004578.1 NA NA NA -2.28565 NA NAPSPTO4718 NC_004578.1 NA NA NA -1.992004 NA NAPSPTO4727 NC_004578.1 NA NA NA -3.526454 NA NAPSPTO4766 NC_004578.1 NA NA NA -1.070108 NA NAPSPTO5255 NC_004578.1 NA NA NA -0.761021 NA NAPSPTO5256 NC_004578.1 NA NA NA -1.578395 NA NAPSPTO5354 NC_004578.1 NA NA NA -1.151489 NA NAPSPTO5377 NC_004578.1 NA NA NA 2.8623793 NA NAPSPTO5378 NC_004578.1 NA 3.8950923 NA 3.2728285 NA NAPSPTO5379 NC_004578.1 NA 2.5138799 NA 1.6877617 NA NAPSPTO5380 NC_004578.1 NA 3.2082837 NA 2.8727084 NA NAPSPTO5381 NC_004578.1 NA 3.7296646 NA 3.0217049 NA NAPSPTO_B0005 NC_004632.1 NA NA NA -0.896596 NA NAPSPTO_B0026 NC_004632.1 NA NA NA -0.777345 NA NAPSPTOA0012 NC_004633.1 NA NA NA -1.373186 NA NAPSPTOA0017 NC_004633.1 NA NA NA -0.898187 NA NAPSPTOA0018 NC_004633.1 NA NA NA -0.885862 NA NAPSPTOA0019 NC_004633.1 NA NA NA -1.21726 NA NA

Page 189: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

c-/c+ b+/c+ nameNA NA hopY1NA NA5.2431938 NA tonB-16.4724107 NA exbD-18.8815456 NA exbB-1NA NA iucDNA NANA NANA NANA NA iaaLNA NA shcFNA NANA NA apaHNA NANA NANA NA hopH1NA NA hopC1NA NA rplXNA NA rplENA NA rpmJNA NANA NANA NA fecB-2.631302 NA-1.869806 NA hopAJ1

NA NANA NANA NA hopD1-1.889711 NA hopQ1-1

NA NA hopR1NA NANA NA fruKNA NANA NA pgl-1.316473 NA-2.227402 NA hopN1

NA NANA NA hopAA1-1NA NA hrpW1NA NA shcMNA NA hopM1NA NA avrE1-2.406927 NA

NA NA hrpZ1NA NA hrpB(Pto)NA NA hrcJ-1.611665 NA hrpD-2.790877 NA hrpE

NA NA hrpF-1.393513 NA hrpG-1.425796 NA hrcC

NA NA hrpT-1.779791 NA hrpV

NA NA hrcR-1.888265 NA hrcQb-2.364174 NA hrcQa

: Differentially regulated genes identified at a p value less than or equal to 0.0004 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 190: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

-1.652615 NA hrpP-1.735737 NA hrpO-4.469206 NA hrcN-2.537096 NA hrpQ

NA NA hrcV-2.508559 NA hrpJ-1.729669 NA hrpL

NA NA hrpK1NA NA hopB1-2.976955 NA

NA NA cumANA NA trmD-4.379087 NA hopAF1-0.761407 NA

NA NANA NANA NA9.0235798 NA4.4037076 NA11.478055 NA-1.724496 NA pcaG

NA NA infCNA NA

10.3148 NA irp110.275206 NA9.3737924 NANA NA hopP1NA NANA NA-1.072279 NA hopAB21.9114979 NA zwf-22.0177668 NA gnd7.3413133 NA6.0026651 NANA NA infANA NA clpA-2.138914 NA-1.220539 NA6.0741522 NANA NA katB5.9791688 NA

6.006367 NANA NANA NA nadANA NA hopAK1NA NA capB8.6726328 NANA NA bfrNA NA glpKNA NANA NANA 2.384627NA -1.902473-0.778112 NA hopE1-1.637949 NA

NA NANA NANA NA

Page 191: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

NA NANA NANA NA

-1.97661 NA hopS2NA NA shcS2-3.303099 NA hopS1-1.609763 NA shcS1

NA NA hopAD1NA NA hopAA1-2NA NA hopG1NA NANA NA cynTNA NA-1.565909 NA hopA1

NA NANA NANA NANA NANA NANA NA plcA2NA NA-1.478059 NA HopX1

NA NA shcO1-0.881881 NA hopO1-1

-1.70248 NA hopT1-1

Page 192: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

annotationtype III effector HopY1citrate transportertonB proteinTonB system transport protein ExbDTonB system transport protein ExbBL-lysine 6-monooxygenasehypothetical proteinhypothetical proteiniron ABC transporter, periplasmic iron-binding proteinindoleacetate-lysine ligasetype III chaperone protein ShcFhypothetical proteindiadenosinetetraphosphataseautotransporting lipase, GDSL familytranscriptional regulator PrtN, putativetype III effector HopH1type III effector HopC150S ribosomal protein L2450S ribosomal protein L550S ribosomal protein L36bacterioferritinaldehyde dehydrogenase family proteiniron(III) dicitrate transport system, periplasmic iron-binding protein FecBhypothetical proteintype III effector HopAJ1nikkomycin biosynthesis domain proteinhypothetical proteintype III effector HopD1type III effector HopQ1-1type III effector HopR1phosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components1-phosphofructokinaseDNA-binding response regulator6-phosphogluconolactonaseconserved effector locus proteintype III effector HopN1conserved effector locus proteintype III effector HopAA1-1type III helper protein HrpW1type III chaperone ShcMtype III effector HopM1type III effector protein AvrE1membrane-bound lytic murein transglycosylase D, putativetype III helper protein HrpZ1type III secretion protein HrpB(Pto)type III secretion protein HrcJtype III secretion protein HrpDtype III secretion protein HrpEtype III secretion protein HrpFtype III secretion protein HrpGouter-membrane type III secretion protein HrcCtype III secretion protein HrpTnegative regulator of hrp expression HrpVtype III secretion protein HrcRtype III secretion protein HrcQbtype III secretion protein HrcQa

: Differentially regulated genes identified at a p value less than or equal to 0.0004 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 193: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

type III secretion protein HrpPtype III secretion protein HrpOtype III secretion cytoplasmic ATPase HrcNtype III secretion protein HrpQtype III secretion protein HrcVtype III secretion protein HrpJRNA polymerase sigma factor HrpLtype III helper protein HrpK1type III effector HopB1hypothetical proteinmulticopper oxidasetRNA (guanine-N(1)-)-methyltransferasetype III effector HopAF1hypothetical proteinaromatic amino acid permeaseresponse regulatorDNA-binding response regulator, LuxR familyMbtH-like proteinhypothetical proteinTonB-dependent siderophore receptor, putativeprotocatechuate 3,4-dioxygenase, alpha subunittranslation initiation factor IF-3hypothetical proteinyersiniabactin polyketide non-ribosomal peptide synthetaseyersiniabactin non-ribosomal peptide synthetaseTonB-dependent siderophore receptor, putativetype III helper protein HopP1enoyl-CoA hydrataseTonB-dependent receptor, putativetype III effector HopAB2glucose-6-phosphate 1-dehydrogenase6-phosphogluconate dehydrogenasehypothetical proteinTonB-dependent siderophore receptor, putativetranslation initiation factor IF-1ATP-dependent clp protease, ATP-binding subunit ClpADNA-binding response regulatorlipoprotein, putativeTonB-dependent siderophore receptor, putativecatalasedyp-type peroxidase family proteinhypothetical proteinhypothetical proteinquinolinate synthetasetype III effector HopAK1cold shock protein CapBbacterioferritin-associated ferredoxinbacterioferritinglycerol kinaseTctC protein, putativemembrane protein TctB, putativemembrane protein TctA, putativehypothetical proteintype III effector HopE1moxR protein, putativeiron-regulated protein A, putativelipoprotein, putativelipoprotein, putative

Page 194: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

lipoprotein, putativehypothetical proteintoluene tolerance protein, putativetype III effector HopS2type III chaperone ShcS2type III effector HopS1type III chaperone ShcS1type III effector HopAD1type III effector HopAA1-2type III effector HopG1hypothetical proteincarbonic anhydrasesulfate transporter family proteintype III effector HopA1hypothetical proteinhypothetical proteinhypothetical proteinallophanate hydrolase, putativebiotin carboxylase biotin carboxyl carrier proteinphosphoesterase family proteinhypothetical proteintype III effector HopX1type III chaperone ShcO1type III effector HopO1-1type III effector HopT1-1

Page 195: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

notesPreviously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to GP:14595286, and GP:14595286; identified by sequence similarity; putativesimilar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putativesimilar to GP:14595284; identified by sequence similarity; putativesimilar to SP:P11295; identified by sequence similarity; putativeidentified by Glimmer2; putativeidentified by Glimmer2; putative

similar to SP:P18204, GB:J04031, SP:P11586, and PID:307178; identified by sequence similarity; putative

similar to SP:P77391; identified by sequence similarity; putativeCatalyzes the hydrolysis of P1,P4-bis(5 -adenosyl) tetraphosphate

previously known as HopPtoH (PMID 12032338; Petnicki-Ocwieja et al, 2002).previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586Found in the ribonucleoprotein core and is involved in the early assembly of the 50S subunitMediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberanceRibosomal protein L36 is the smallest protein from the large subunit of the prokaryotic ribosome

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putativesimilar to SP:P77262; identified by sequence similarity; putativepreviously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putativesimilar to GP:14030855; identified by sequence similarity; putativeAlso known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

catalyzes the formation of 6-phospho-D-gluconate from 6-phospho-D-glucono-1,5-lactonesimilar to GP:8037800; identified by sequence similarity; putativeAlso known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586similar to GP:8037798, SP:P32109, GB:U15124, and PID:563996; identified by sequence similarity; putativepreviously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987similar to GP:3694999, and GP:8037796; identified by sequence similarity; putative

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putativesimilar to SP:P23931; identified by sequence similarity; putativesimilar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3603316, and GP:9800449; identified by sequence similarity; putativesimilar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putativesimilar to GP:3228545, GB:U09067, PID:483876, and PID:553456; identified by sequence similarity; putativesimilar to GP:3603319, and GP:3228546; identified by sequence similarity; putativesimilar to GP:3228547, GB:M96789, SP:P35212, and PID:183223; identified by sequence similarity; putativesimilar to GP:3603321, and GP:3603255; identified by sequence similarity; putativesimilar to GP:3603256, and GP:3228549; identified by sequence similarity; putativesimilar to GP:11276516; identified by sequence similarity; putativesimilar to GP:11276515, and GP:11276515; identified by sequence similarity; putativesimilar to GP:3282779, and GP:11276514; identified by sequence similarity; putative

: Differentially regulated genes identified at a p value less than or equal to 0.0004 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log

Page 196: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:11276513, GB:L22846, SP:Q14209, and PID:410207; identified by sequence similarity; putativesimilar to GP:3282777, and GP:11276512; identified by sequence similarity; putativesimilar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putativesimilar to GP:11276510; identified by sequence similarity; putativesimilar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putativesimilar to GP:5360281, and SP:P37929; identified by sequence similarity; putativesimilar to GP:8037778, and GP:8037778; identified by sequence similarity; putativeAlso known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putativeidentified by Glimmer2; putative

methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNApreviously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)identified by Glimmer2; putativesimilar to SP:P15993; identified by sequence similarity; putative

similar to GP:15159638; identified by sequence similarity; putativeidentified by Glimmer2; putativesimilar to SP:P42512, GB:L17325, and PID:306323; identified by sequence similarity; putativesimilar to GP:10442739, and SP:P00436; identified by sequence similarity; putativeBinds to the 30S ribosomal subunit and enhances its availability for the initiation of protein synthesisidentified by Glimmer2; putativeThis synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putativepreviously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putativeCatalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoAidentified by match to TIGR protein family HMM TIGR01783also known as AvrPtoB; similar to GP:5702216, and GP:18535643; identified by sequence similarity; putative

catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconateidentified by Glimmer2; putativesimilar to GP:2981048, and SP:P00089; identified by sequence similarity; putativeStimulates the activities of the other two initiation factors, IF-2 and IF-3

identified by match to TIGR protein family HMM TIGR01783similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF04261identified by match to PFAM protein family HMM PF04302identified by Glimmer2; putative3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphatepreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putativesimilar to GP:13625473, and SP:P80415; identified by sequence similarity; putativesimilar to GP:4378826, and SP:P13655; identified by sequence similarity; putativesimilar to SP:P22759, and SP:P22759; identified by sequence similarity; putativeConverts glycerol and ADP to glycerol-3-phosphate and ADPsimilar to GP:11128402; identified by sequence similarity; putativesimilar to GP:11128403; identified by sequence similarity; putativesimilar to GP:11128404, and GP:11128404; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).similar to GP:7799213; identified by sequence similarity; putative

Page 197: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:9950620; identified by sequence similarity; putativesimilar to GP:4336803; identified by sequence similarity; putativePreviously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).identified by Glimmer2; putativePreviously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putativeidentified by Glimmer2; putativePreviously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).The C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putativesimilar to GP:12544544, and GP:15159386; identified by sequence similarity; putativeidentified by match to PFAM protein family HMM PF03746identified by Glimmer2; putativesimilar to GP:2290992; identified by sequence similarity; putativesimilar to GB:X74143, SP:P55316, PID:516383, and PID:967048; identified by sequence similarity; putativesimilar to GP:8572766; identified by sequence similarity; putativeidentified by Glimmer2; putativeAlso known as AvrPphE; similar to GP:571514; identified by sequence similarity; putativeidentified by Glimmer2; putativePreviously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 198: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as HolPtoY (PMID 11872842; Guttman et al, 2002) and ORF11 (PMID 11854524; Fouts et al, 2002).; similar to GP:19071534; identified by sequence similarity; putative

similar to SP:Q05606, GB:X60188, SP:P27361, SP:P28482, PID:1335009, PID:186696, and PID:31221; identified by sequence similarity; putative

previously known as HopPtoC (PMID 12032338; Petnicki-Ocwieja et al, 2002);identified by match to TIGR protein family HMM TIGR01586

Mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putative

previously known as hopPmaG (PMID 11872842; Guttman et al, 2002); similar to GP:19071492; identified by sequence similarity; putative

Also known as Ipx47 (PMID 11967070; Boch et al, 2002).; similar to GP:14030855; identified by sequence similarity; putativepreviously known as HopPtoD1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:14905934; identified by sequence similarity; putativePreviously known as ORF19 (PMID 12032338; Petnicki-Ocwieja et al, 2002) and HolPtoQ (PMID 11872842; Guttman et al, 2002); similar to GP:17427254, and GP:19071520; identified by sequence similarity; putativePreviously known as HolPtoR; similar to GP:17431754, and GP:19071522; identified by sequence similarity; putative

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as HopPtoA1 (PMID 12437299; Badel et al,2002) and CEL ORF5 (PMID 10781092; Alfano et al, 2000); identified by match to PFAM protein family HMM PF02987

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:9800448, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

similar to GP:790912, GB:U09068, PID:483878, PID:563405, PID:563415, PID:563418, PID:563428, PID:563458, PID:563460, PID:563477, PID:563481, and PID:976302; identified by sequence similarity; putative

: Differentially regulated genes identified at a p value less than or equal to 0.0004 using a GCRMA/FDR analyses. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3. All fold changes are reported in log 2.

Page 199: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putativesimilar to GP:11276508, GB:X73459, GB:U07857, SP:P37108, PID:313661, and PID:468209; identified by sequence similarity; putative

Also known as EEL ORF1 (PMID 10781092; Alfano et al, 2000) and HopPtoB (PMID 11872842; Guttman et al, 2002).; similar to GP:8037777; identified by sequence similarity; putative

previously known as HolPtoN (PMID 11872842; Guttman et al, 2002) and HopPtoJ (PMID 12032338; Petnicki-Ocwieja et al, 2002)

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putativePresumed to have relevance to siderophore functions due to presence at one end of the yersiniabactin biosynthesis operon.; similar to GP:557754, and SP:P46359; identified by sequence similarity; putativepreviously known as HopPtoP (PMID 11872842; Guttman et al, 2002) and HrpW-related (PMID 11854524; Fouts et al, 2002); similar to GP:3694999; identified by sequence similarity; putative

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphatepreviously known as HopPmaH (PMID 11872842; Guttman et al, 2002); similar to GP:1783275, and GP:19071494; identified by sequence similarity; putative

previously known as HolPtoV (PMID 11872842; Guttman et al, 2002) and HopPtoE (PMID 12032338; Petnicki-Ocwieja et al, 2002).

Page 200: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as ORF15 (PMID 12032338; Petnicki-Ocwieja et al 2002) and HolPtoZ2 (PMID 12615215; Greenberg and Vinatzer, 2003).

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

Previously known as HolPtoS (PMID 11872842; Guttman et al, 2002) and HopPtoI (PMID 12032338; Petnicki-Ocwieja et al, 2002); identified by match to PFAM protein family HMM PF02918previously known as HopPtoA2 (PMID 12437299; Badel et al,2002); identified by match to PFAM protein family HMM PF02987Previously known as HolPtoW (PMID 11872842; Guttman et al, 2002) and HopPtoG (PMID 12032338; Petnicki-Ocwieja et al, 2002).The C-terminal residues of this ORF are encoded by an adjacent insertion sequence.; identified by Glimmer2; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

Previously known as HopPtoO (PMID 11872842; Guttman et al, 2002) and HopPtoS1 (PMID 12032338; Petnicki-Ocwieja et al, 2002); similar to GP:19071512; identified by sequence similarity; putativePreviously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 201: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to SP:P15028, GB:M62925, GB:D90287, GB:M55183, GB:X57974, GB:M98447, SP:P22735, PID:1256959, PID:186790, PID:219632, PID:339527, PID:339604, and PID:510525; identified by sequence similarity; putative

Also known as CEL ORF7 (PMID 10781092; Alfano et al, 2000) and HolPtoT (PMID 11872842; Guttman et al, 2002), and HopPtoN (PMID 15469508; Lopez-Solanilla, et al, 2004); identified by match to TIGR protein family HMM TIGR01586

previously known as CEL ORF3 (PMID 10781092; Alfano et al, 2000) and HolPtoX (PMID 11872842; Guttman et al, 2002) and HopPtoM (PMID 12940984; Badel et al, 2003); similar to GP:8037794; identified by sequence similarity; putativesimilar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 202: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GP:11276511, GB:J04478, GB:M11718, GB:X04758, GB:M10956, GB:M11135, SP:P05997, PID:1340175, PID:179694, PID:179698, PID:180428, PID:180913, PID:2370202, and PID:553235; identified by sequence similarity; putative

similar to GP:11276509, GB:M27160, GB:M63235, GB:M63236, GB:M63237, GB:M63238, GB:M63239, GB:Y00819, GB:J03581, GB:U01873, SP:P14679, PID:340035, PID:340037, PID:340040, PID:37507, PID:37509, and PID:403422; identified by sequence similarity; putative

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

Page 203: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Previously known as holPtoZ (PMID 11872842; Guttman et al, 2002), HopPtoS4 (PMID 14702323; Schechter, 2004)ORF26 (PMID 12032338; Petnicki-Ocwieja et al, 2002).; similar to GP:19071536; identified by sequence similarity; putative

previously known as HrmA (PMID 8274770; Heu and Hutcheson, 1993) and HopPsyA (PMID 11854524; Fouts et al, 2002); similar to SP:Q08370, GB:L05500, SP:Q08828, and PID:349269; identified by sequence similarity; putative

Previously known as ORF16 (PMID 12032338; Petnicki-Ocwieja et al, 2002), HolPtoU (PMID 11872842; Guttman et al, 2002) and HopPtoT (PMID 14702323; Schechter, 2004); similar to GP:19071526; identified by sequence similarity; putative

Page 204: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 205: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

This synthetase catalyzes the final steps in the biosynthesis of the siderophore yersiniabactin, adding one acetate unit with concomitant reduction to the alcohol and dimethylation followed by the addition, cyclization and methylation of one cysteine residue. The final product is released by the terminal thioesterase domain.; similar to GP:4106636; identified by sequence similarity; putativeCatalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

similar to SP:P46206, GB:M11958, GB:M11959, GB:M11960, GB:M11961, GB:M11962, GB:M11963, GB:M11964, GB:M11965, GB:M11966, GB:M11967, GB:M11968, GB:L00159, GB:L00160, GB:S75476, GB:V00572, GB:D28371, SP:P00558, SP:P07205, PID:35435, PID:387020, and PID:387021; identified by sequence similarity; putative

Page 206: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 207: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 208: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 209: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 210: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

similar to GB:K02096, GB:X66038, GB:X66039, GB:X66037, GB:X93626, SP:P01600, SP:P01602, SP:P01606, SP:P04431, PID:186006, PID:33150, PID:33307, PID:33311, PID:33313, PID:470592, PID:470594, PID:470596, PID:470600, PID:470602, PID:470604, PID:470606, PID:470608, PID:470610, PID:470612, PID:506423, PID:567136, PID:567138, PID:567154, PID:567158, PID:567168, PID:567172, PID:587326, PID:587328, PID:619603, PID:619613, PID:619614, PID:619624, PID:663000, PID:663001, PID:722458, PID:722540, PID:722552, PID:732746, PID:758085, PID:758589, PID:758599, PID:790811, PID:791024, PID:791036, PID:860994, PID:861002, and PID:940528; identified by sequence similarity; putative

similar to GP:790908, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putativesimilar to GP:790909, GB:U09066, SP:P01768, SP:P01769, SP:P01770, SP:P01771, SP:P01772, PID:483874, PID:488294, PID:496012, PID:496026, PID:499604, PID:553396, PID:553398, PID:553399, PID:553408, PID:553434, PID:553435, PID:553436, PID:553437, PID:553438, PID:553439, PID:553440, PID:553443, PID:553445, PID:553455, PID:567123, PID:567126, PID:567127, PID:587294, PID:587296, PID:587312, PID:618468, PID:619425, PID:619629, PID:619630, PID:758094, PID:773600, PID:790797, PID:791026, PID:901824, PID:901825, PID:940526, PID:945217, PID:963049, PID:976304, PID:976311, PID:976315, and PID:976342; identified by sequence similarity; putative

Page 211: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Catalyzes the condensation of salicylate with two molecules of cysteine which are both cyclized to thiazoline rings. This enzyme contains a single adenylation domain which most likely charges both of final two thiolation domains with cysteine. Following the adenylation domain is an unidentified domain which most likely provides the docking site for the thiazoline reductase (irp3) which reduces the second thiazoline ring. The product of this synthetase may be released in trans by the thioesterase component (irp4) or directly transferred to the hybrid synthetase (irp1) for the final steps of yersiniabactin biosynthesis.; similar to SP:P48633, and GP:4106635; identified by sequence similarity; putative

Page 212: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Cluster OrderDiscussion ClusterNode Locus_tag Regulatory Motif Gene ID1 I 1.1.1.1.1.1 PSPTO_0954 2 I 1.1.1.1.1.1 PSPTO_0955 fruK 3 I 1.1.1.1.1.1 PSPTO_0883 HrpL hopR1 4 I 1.1.1.1.1.1 PSPTO_4530 katG 5 I 1.1.1.1.1.1 PSPTO_0851 6 I 1.1.1.1.1.1 PSPTO_1403 HrpL hrpJ 7 I 1.1.1.1.1.1 PSPTO_A0018 HrpL hopO1-1 8 I 1.1.1.1.1.2 PSPTO_1391 HrpL hrpV 9 I 1.1.1.1.1.2 PSPTO_1390 HrpL hrpT

10 I 1.1.1.1.1.2 PSPTO_1396 HrpL hrcQb 11 I 1.1.1.1.1.2 PSPTO_0852 HrpL hopAJ1 12 I 1.1.1.1.1.2 PSPTO_0877 HrpL hopQ1-1 13 I 1.1.1.1.1.2 PSPTO_1400 HrpL hrcN 14 I 1.1.1.1.1.2 PSPTO_1402 HrpL hrcV 15 I 1.1.1.1.1.2 PSPTO_0876 HrpL hopD1 16 I 1.1.1.1.1.2 PSPTO_4101 HrpL hopAK1 17 I 1.1.1.1.1.2 PSPTO_1401 HrpL hrpQ 18 I 1.1.1.1.1.2 PSPTO_3087 HrpL hopAB2 19 I 1.1.1.1.1.2 PSPTO_4599 HrpL shcS1 20 I 1.1.1.1.1.2 PSPTO_0653 21 I 1.1.1.1.1.2 PSPTO_1380 hrpS 22 I 1.1.1.1.1.2 PSPTO_3582 katB 23 I 1.1.1.1.1.2 PSPTO_0588 HrpL hopH1 24 I 1.1.1.1.1.2 PSPTO_0524 HrpL 25 I 1.1.1.1.1.2 PSPTO_1568 HrpL hopAF1 26 I 1.1.1.1.1.2 PSPTO_4160 bfr 27 I 1.1.1.1.1.2 PSPTO_1404 hrpL 28 I 1.1.1.1.1.2 PSPTO_1398 HrpL hrpP 29 I 1.1.1.1.1.2 PSPTO_A0017 HrpL shc01 30 I 1.1.1.1.1.2 PSPTO_0044 HrpL hopK1 31 I 1.1.1.1.1.2 PSPTO_4703 HrpL hopAQ1 32 I 1.1.1.1.1.2 PSPTO_4704 corR 33 I 1.1.1.1.1.2 PSPTO_1375 HrpL hopM1 34 I 1.1.1.1.1.2 PSPTO_0503 HrpL shcF 35 I 1.1.1.1.1.2 PSPTO_1369 HrpL shcN36 I 1.1.1.1.1.2 PSPTO_1389 HrpL hrcC 37 I 1.1.1.1.1.2 PSPTO_B0005 HrpL plcA2 38 I 1.1.1.1.1.2 PSPTO_0875 39 I 1.1.1.1.1.2 PSPTO_1374 HrpL shcM 40 I 1.1.1.1.1.2 PSPTO_4776 HrpL hopI1 41 I 1.1.1.1.1.2 PSPTO_1395 HrpL hrcR 42 I 1.1.1.1.1.2 PSPTO_A0012 HrpL HopX1 43 I 1.1.1.1.1.2 PSPTO_4718 HrpL hopAA1-244 I 1.1.1.1.1.2 PSPTO_1405 HrpL hrpK1 45 I 1.1.1.1.1.2 PSPTO_4589 HrpL shcS2 46 I 1.1.1.1.1.2 PSPTO_1371 47 I 1.1.1.1.1.2 PSPTO_0994 48 I 1.1.1.1.1.2 PSPTO_0061 HrpL hopY1 49 I 1.1.1.1.1.2 PSPTO_1386 HrpL hrpE 50 I 1.1.1.1.1.2 PSPTO_1378 HrpL hrpH51 I 1.1.1.1.1.2 PSPTO_0589 HrpL hopC1 52 I 1.1.1.1.1.2 PSPTO_1397 HrpL hrcQa 53 I 1.1.1.1.1.2 PSPTO_3381 54 I 1.1.1.1.1.2 PSPTO_1370 HrpL hopN1 55 I 1.1.1.1.1.2 PSPTO_2130 HrpL 56 I 1.1.1.1.1.2 PSPTO_0855

Supplemental Table 5: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses sorted based on their order in the clustering analysis seen in Figure 5A. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3.

Page 213: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

57 I 1.1.1.1.1.2 PSPTO_1372 HrpL hopAA1-158 I 1.1.1.1.1.2 PSPTO_2128 HrpL 59 I 1.1.1.1.1.2 PSPTO_4333 60 I 1.1.1.1.1.2 PSPTO_1406 HrpL hopB1 61 I 1.1.1.1.1.2 PSPTO_2678 HrpL hopP1 62 I 1.1.1.1.1.2 PSPTO_1377 HrpL avrE1 63 I 1.1.1.1.1.2 PSPTO_4588 HrpL hopS2 64 I 1.1.1.1.1.2 PSPTO_5255 cynT 65 I 1.1.1.1.1.2 PSPTO_4727 HrpL hopG1 66 I 1.1.1.1.1.2 PSPTO_1609 67 I 1.1.1.1.1.2 PSPTO_4766 68 I 1.1.1.1.1.2 PSPTO_5256 69 I 1.1.1.1.1.2 PSPTO_2047 70 I 1.1.1.1.1.2 PSPTO_1379 hrpR 71 I 1.1.1.1.1.2 PSPTO_1388 HrpL hrpG 72 I 1.1.1.1.1.2 PSPTO_4363 RpoD sodB 73 I 1.1.1.1.1.2 PSPTO_1408 HrpL 74 I 1.1.1.1.1.2 PSPTO_1387 HrpL hrpF 75 I 1.1.1.1.1.2 PSPTO_5355 76 I 1.1.1.1.1.2 PSPTO_3959 nadA 77 I 1.1.1.1.1.2 PSPTO_4597 HrpL hopS1 78 I 1.1.1.1.1.2 PSPTO_1383 HrpL hrpB(Pto)79 I 1.1.1.1.1.2 PSPTO_1384 HrpL hrcJ 80 I 1.1.1.1.1.2 PSPTO_1399 HrpL hrpO 81 I 1.1.1.1.1.2 PSPTO_2339 pcaG 82 I 1.1.1.1.1.2 PSPTO_A0019 HrpL hopT1-1 83 I 1.1.1.1.1.2 PSPTO_3382 84 I 1.1.1.1.1.2 PSPTO_2105 HrpL 85 I 1.1.1.1.1.2 PSPTO_4331 HrpL hopE1 86 I 1.1.1.1.1.2 PSPTO_2719 87 I 1.1.1.1.1.2 PSPTO_5354 HrpL hopA1 88 I 1.1.1.1.1.2 PSPTO_1385 HrpL hrpD 89 I 1.1.1.1.1.2 PSPTO_3380 90 I 1.1.1.1.1.2 PSPTO_4733 HrpL 91 I 1.1.1.1.1.2 PSPTO_4647 cioB 92 II 1.1.1.1.2 PSPTO_0598 RpoD speD 93 II 1.1.1.1.2 PSPTO_1409 HrpL 94 II 1.1.1.1.2 PSPTO_0165 95 II 1.1.1.1.2 PSPTO_2198 sdhB 96 II 1.1.1.1.2 PSPTO_0961 RpoD panB 97 II 1.1.1.1.2 PSPTO_1509 adk 98 II 1.1.1.1.2 PSPTO_5620 HrpL 99 II 1.1.1.1.2 PSPTO_0603

100 II 1.1.1.1.2 PSPTO_0806 RpoD ileS 101 II 1.1.1.1.2 PSPTO_2195 sdhC 102 II 1.1.1.1.2 PSPTO_4562 103 II 1.1.1.1.2 PSPTO_2904 vanA 104 II 1.1.1.1.2 PSPTO_3368 nuoE 105 II 1.1.1.1.2 PSPTO_4648 cioA 106 II 1.1.1.1.2 PSPTO_2196 prrF2 107 II 1.1.1.1.2 PSPTO_3815 accD 108 II 1.1.1.1.2 PSPTO_5353 HrpL shcA 109 II 1.1.1.1.2 PSPTO_5474 rubA 110 II 1.1.1.1.2 PSPTO_3162 111 II 1.1.1.1.2 PSPTO_2275 aroF-1 112 II 1.1.1.1.2 PSPTO_4444 RpoD 113 II 1.1.1.1.2 PSPTO_3830 RpoD fabF 114 II 1.1.1.1.2 PSPTO_2338 pcaH

Page 214: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

115 II 1.1.1.1.2 PSPTO_2280 cysH 116 II 1.1.1.1.2 PSPTO_B0012 117 II 1.1.1.1.2 PSPTO_4956 118 II 1.1.1.1.2 PSPTO_4332 119 II 1.1.1.2 PSPTO_3337 120 II 1.1.1.2 PSPTO_3364 aceA 121 1.1.2.1 PSPTO_0834 HrpL 122 1.1.2.1 PSPTO_0836 HrpL 123 1.1.2.1 PSPTO_0837 HrpL 124 1.1.2.1 PSPTO_0835 HrpL 125 1.1.2.1 PSPTO_0838 HrpL 126 1.1.2.1 PSPTO_0874 127 1.1.2.1 PSPTO_2691 128 III 1.1.2.2 PSPTO_1289 glk 129 III 1.1.2.2 PSPTO_1778 htpX 130 III 1.1.2.2 PSPTO_0679 131 III 1.1.2.2 PSPTO_4174 132 III 1.1.2.2 PSPTO_4168 glpK 133 III 1.1.2.2 PSPTO_0022 134 III 1.1.2.2 PSPTO_0545 135 III 1.1.2.2 PSPTO_0594 trpC 136 III 1.1.2.2 PSPTO_0940 terZ 137 III 1.1.2.2 PSPTO_2806 138 III 1.1.2.2 PSPTO_3355 139 III 1.1.2.2 PSPTO_5621 140 III 1.1.2.2 PSPTO_A0011 141 III 1.1.2.2 PSPTO_1817 RpoD 142 III 1.1.2.2 PSPTO_4687 cfa7 143 III 1.1.2.2 PSPTO_0206 144 III 1.1.2.2 PSPTO_0546 145 III 1.1.2.2 PSPTO_5622 HrpL 146 III 1.1.2.2 PSPTO_0727 eutB 147 III 1.1.2.2 PSPTO_A0008 148 III 1.1.2.2 PSPTO_4685 cfa5 149 III 1.1.2.2 PSPTO_1382 HrpL hrpZ1 150 III 1.1.2.2 PSPTO_4173 151 III 1.1.2.2 PSPTO_4690 cfa9 152 III 1.1.2.2 PSPTO_3039 153 III 1.1.2.2 PSPTO_4721 HrpL shcV 154 III 1.1.2.2 PSPTO_0959 pgi 155 III 1.1.2.2 PSPTO_1855 156 III 1.1.2.2 PSPTO_0703 157 III 1.1.2.2 PSPTO_0873 158 III 1.1.2.2 PSPTO_5522 HrpL 159 III 1.1.2.2 PSPTO_3987 oprD 160 III 1.1.2.2 PSPTO_2844 161 III 1.1.2.2 PSPTO_B0027 162 III 1.1.2.2 PSPTO_2853 163 III 1.1.2.2 PSPTO_B0025 164 III 1.1.2.2 PSPTO_1213 165 III 1.1.2.2 PSPTO_5466 166 III 1.1.2.2 PSPTO_2208 htpG 167 III 1.1.2.2 PSPTO_4285 adhB 168 III 1.1.2.2 PSPTO_1296 oprB 169 III 1.1.2.2 PSPTO_4646 170 III 1.1.2.2 PSPTO_4339 171 III 1.1.2.2 PSPTO_4686 cfa6 172 III 1.1.2.2 PSPTO_4358

Page 215: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

173 III 1.1.2.2 PSPTO_2702 xylB 174 III 1.1.2.2 PSPTO_1708 cobO 175 III 1.1.2.2 PSPTO_2680 gabD-3 176 III 1.1.2.2 PSPTO_4507 recN 177 III 1.1.2.2 PSPTO_5517 178 III 1.1.2.2 PSPTO_3269 pstS 179 III 1.1.2.2 PSPTO_2638 abP 180 III 1.1.2.2 PSPTO_B0026 181 III 1.1.2.2 PSPTO_2845 182 III 1.1.2.2 PSPTO_4955 RpoD psd 183 III 1.1.2.2 PSPTO_5407 184 III 1.1.2.2 PSPTO_A0009 185 III 1.1.2.2 PSPTO_4720 HrpL hopV1 186 III 1.1.2.2 PSPTO_3893 187 III 1.1.2.2 PSPTO_4033 recA 188 III 1.1.2.2 PSPTO_4691 hopAD1 189 IV 1.2.1.1 PSPTO_1214 190 iV 1.2.1.1 PSPTO_1287 gap-1 191 IV 1.2.1.1 PSPTO_1721 RpoD 192 IV 1.2.1.1 PSPTO_2589 193 IV 1.2.1.1 PSPTO_0570 194 IV 1.2.1.1 PSPTO_4297 195 IV 1.2.1.2 PSPTO_0371 HrpL iaaL 196 IV 1.2.1.2 PSPTO_1288 edd 197 IV 1.2.1.2 PSPTO_1373 HrpL hrpW1 198 IV 1.2.1.2 PSPTO_0328 ompR 199 IV 1.2.1.2 PSPTO_1290 200 IV 1.2.1.2 PSPTO_2850 201 IV 1.2.1.2 PSPTO_0569 202 IV 1.2.1.2 PSPTO_0231 203 IV 1.2.1.2 PSPTO_3550 fahA 204 IV 1.2.1.2 PSPTO_0728 205 IV 1.2.1.2 PSPTO_3493 206 IV 1.2.1.2 PSPTO_3495 207 IV 1.2.1.2 PSPTO_3278 208 IV 1.2.1.2 PSPTO_1302 eda-1 209 IV 1.2.1.2 PSPTO_0944 terD 210 IV 1.2.1.2 PSPTO_0547 211 IV 1.2.1.2 PSPTO_3291 212 IV 1.2.1.2 PSPTO_5147 213 IV 1.2.1.2 PSPTO_1301 pgl 214 IV 1.2.1.2 PSPTO_3282 215 IV 1.2.1.2 PSPTO_1300 zwf-1 216 IV 1.2.1.2 PSPTO_1565 rpoS 217 IV 1.2.1.2 PSPTO_3925 218 IV 1.2.1.2 PSPTO_3551 hmgA 219 IV 1.2.1.2 PSPTO_2707 220 IV 1.2.1.2 PSPTO_3353 clpA 221 IV 1.2.1.2 PSPTO_3553 hppD 222 IV 1.2.1.2 PSPTO_0853 223 IV 1.2.1.2 PSPTO_1724 224 IV 1.2.1.2 PSPTO_2720 nudC 225 IV 1.2.1.2 PSPTO_3333 226 IV 1.2.1.2 PSPTO_0776 recC 227 IV 1.2.1.2 PSPTO_3544 228 IV 1.2.1.2 PSPTO_3455 229 IV 1.2.1.2 PSPTO_4560 230 V 1.2.2 PSPTO_0087

Page 216: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

231 V 1.2.2 PSPTO_1148 alkK 232 V 1.2.2 PSPTO_2274 233 V 1.2.2 PSPTO_0351 234 V 1.2.2 PSPTO_0499 235 V 1.2.2 PSPTO_1930 cynS 236 V 1.2.2 PSPTO_4380 fabG 237 V 1.2.2 PSPTO_4557 238 V 1.2.2 PSPTO_2331 239 V 1.2.2 PSPTO_1340 240 V 1.2.2 PSPTO_3323 241 V 1.2.2 PSPTO_0217 glnK 242 V 1.2.2 PSPTO_B0010 243 V 1.2.2 PSPTO_4306 pcaT 244 V 1.2.2 PSPTO_0927 245 V 1.2.2 PSPTO_4762 246 V 1.2.2 PSPTO_4108 247 V 1.2.2 PSPTO_4582 248 V 1.2.2 PSPTO_2705 249 V 1.2.2 PSPTO_2752 tpx 250 V 1.2.2 PSPTO_4558 251 VI 2.1.1.1.1.1 PSPTO_5141 hslU 252 VI 2.1.1.1.1.1 PSPTO_5325 RpoD 253 VI 2.1.1.1.1.1 PSPTO_4494 RpoD tpiA 254 VI 2.1.1.1.1.1 PSPTO_3733 RpoD folD-2 255 VI 2.1.1.1.1.2 PSPTO_4573 256 VI 2.1.1.1.1.2 PSPTO_4452 RpoD 257 VI 2.1.1.1.1.2 PSPTO_4407 murC 258 VI 2.1.1.1.1.2 PSPTO_4473 gatC 259 VI 2.1.1.1.1.2 PSPTO_5046 260 VI 2.1.1.1.1.2 PSPTO_3352 infA 261 VI 2.1.1.1.1.2 PSPTO_2211 fabA 262 VI 2.1.1.1.1.2 PSPTO_1809 ispZ 263 VI 2.1.1.1.1.2 PSPTO_4423 sspB 264 VI 2.1.1.1.1.2 PSPTO_1102 pth 265 VI 2.1.1.1.2 PSPTO_5377 266 VI 2.1.1.1.2 PSPTO_5380 267 VI 2.1.1.1.2 PSPTO_5378 268 VI 2.1.1.1.2 PSPTO_5381 269 VI 2.1.1.1.2 PSPTO_3836 RpoD 270 VI 2.1.1.1.2 PSPTO_0283 271 VI 2.1.1.1.2 PSPTO_4442 RpoD 272 VI 2.1.1.1.2 PSPTO_5379 273 VI 2.1.1.1.2 PSPTO_0003 RpoD recF 274 VI 2.1.1.1.2 PSPTO_0549 RpoD apaH 275 VI 2.1.1.1.2 PSPTO_0220 276 2.1.1.2.1 PSPTO_3700 277 2.1.1.2.1 PSPTO_1164 278 VII 2.1.1.2.2.1 PSPTO_4484 279 VII 2.1.1.2.2.1 PSPTO_1633 asnB 280 VII 2.1.1.2.2.1 PSPTO_4234 281 VII 2.1.1.2.2.1 PSPTO_4233 282 VII 2.1.1.2.2.1 PSPTO_1304 283 VII 2.1.1.2.2.1 PSPTO_4232 284 VII 2.1.1.2.2.1 PSPTO_0062 285 VII 2.1.1.2.2.1 PSPTO_0330 286 2.1.1.2.2.2 PSPTO_5351 287 2.1.1.2.2.2 PSPTO_5507 288 2.1.1.2.2.2 PSPTO_4503 dapB

Page 217: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

289 2.1.1.2.2.2 PSPTO_0152 osmC 290 2.1.1.2.2.2 PSPTO_0154 291 2.1.1.2.2.2 PSPTO_2379 RpoD infC 292 2.1.1.2.2.2 PSPTO_1475 RpoD trmD 293 2.1.1.2.2.2 PSPTO_4611 294 2.1.1.2.2.2 PSPTO_0307 295 2.1.1.2.2.2 PSPTO_1134 296 2.1.1.2.2.2 PSPTO_0648 RpoD rpsM 297 2.1.1.2.2.2 PSPTO_0651 RpoD rpoA 298 2.1.1.2.2.2 PSPTO_4578 299 2.1.1.2.2.2 PSPTO_0219 300 2.1.1.2.2.2 PSPTO_0156 301 VIII 2.1.2.1.1 PSPTO_0649 RpoD rpsK 302 VIII 2.1.2.1.1 PSPTO_0211 iucD 303 VIII 2.1.2.1.1 PSPTO_3972 tolB 304 VIII 2.1.2.1.1 PSPTO_4807 305 VIII 2.1.2.1.1 PSPTO_0647 RpoD rpmJ 306 VIII 2.1.2.1.1 PSPTO_1456 cumA 307 VIII 2.1.2.1.1 PSPTO_1543 308 VIII 2.1.2.1.1 PSPTO_4224 rpoE 309 VIII 2.1.2.1.1 PSPTO_0677 310 VIII 2.1.2.1.1 PSPTO_0552 RpoD pdxA 311 VIII 2.1.2.1.1 PSPTO_1429 312 VIII 2.1.2.1.1 PSPTO_2380 RpoD rpmI 313 VIII 2.1.2.1.1 PSPTO_2381 RpoD rplT 314 VIII 2.1.2.1.1 PSPTO_0539 rpsU 315 VIII 2.1.2.1.1 PSPTO_0637 RpoD rplX 316 VIII 2.1.2.1.1 PSPTO_0638 RpoD rplE 317 VIII 2.1.2.1.1 PSPTO_3973 tolA 318 VIII 2.1.2.1.1 PSPTO_0621 RpoD rpsL 319 VIII 2.1.2.1.1 PSPTO_3349 ftsK 320 VIII 2.1.2.1.1 PSPTO_2099 321 VIII 2.1.2.1.1 PSPTO_1544 lpxD 322 VIII 2.1.2.1.1 PSPTO_0628 RpoD rplW 323 VIII 2.1.2.1.1 324 VIII 2.1.2.1.1 PSPTO_5614 RpoD rnpA 325 VIII 2.1.2.1.1 PSPTO_4456 326 VIII 2.1.2.1.1 PSPTO_4943 miaA 327 VIII 2.1.2.1.1 PSPTO_4499 RpoD 328 VIII 2.1.2.1.1 PSPTO_0615 RpoD rplK 329 VIII 2.1.2.1.1 PSPTO_1749 cmk 330 VIII 2.1.2.1.1 PSPTO_5154 hisE 331 VIII 2.1.2.1.1 PSPTO_0309 cysT 332 VIII 2.1.2.1.1 PSPTO_0642 RpoD rplR 333 VIII 2.1.2.1.1 PSPTO_4610 334 VIII 2.1.2.1.1 PSPTO_4933 RpoD rpsF 335 VIII 2.1.2.1.1 PSPTO_2298 sigX336 IX 2.1.2.1.2 PSPTO_4368 Fur 337 IX 2.1.2.1.2 PSPTO_4367 Fur 338 IX 2.1.2.1.2 PSPTO_5310 339 IX 2.1.2.1.2 PSPTO_4136 340 IX 2.1.2.1.2 PSPTO_4145 capB 341 IX 2.1.2.1.2 small RNA cobalamin-4 342 IX 2.1.2.1.2 PSPTO_0426 343 IX 2.1.2.1.2 PSPTO_4366 Fur 344 IX 2.1.2.1.2 Fur prrF2345 IX 2.1.2.1.2 PSPTO_3120 Fur 346 IX 2.1.2.1.2 PSPTO_4381 Fur

small RNA P1

small RNA prrF2

Page 218: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

347 IX 2.1.2.1.2 PSPTO_4159 Fur 348 IX 2.1.2.1.2 PSPTO_3574 Fur 349 IX 2.1.2.1.2 PSPTO_3598 Fur 350 IX 2.1.2.1.2 PSPTO_3294 351 IX 2.1.2.1.2 PSPTO_0068 exbD-1 352 IX 2.1.2.1.2 PSPTO_0067 tonB-1 353 IX 2.1.2.1.2 PSPTO_2152 PvdS 354 IX 2.1.2.1.2 PSPTO_3599 Fur 355 IX 2.1.2.1.2 PSPTO_3122 Fur gnd 356 IX 2.1.2.1.2 PSPTO_0069 exbB-1 357 IX 2.1.2.1.2 PSPTO_4369 Fur 358 IX 2.1.2.1.2 PSPTO_0314 Fur 359 X 2.1.2.2.1 PSPTO_0763 fecB 360 X 2.1.2.2.1 PSPTO_3121 Fur zwf-2 361 X 2.1.2.2.1 PSPTO_2137 PvdS 362 X 2.1.2.2.1 PSPTO_2141 PvdS 363 X 2.1.2.2.1 PSPTO_2155 PvdS pvdN364 X 2.1.2.2.1 PSPTO_2597 irp5 365 X 2.1.2.2.1 PSPTO_2603 366 X 2.1.2.2.1 PSPTO_2148 PvdS pvdJ367 X 2.1.2.2.1 PSPTO_2146 PvdS 368 X 2.1.2.2.1 PSPTO_2134 PvdS pvdG369 X 2.1.2.2.1 PSPTO_3462 Fur 370 X 2.1.2.2.1 PSPTO_2598 irp4 371 X 2.1.2.2.1 PSPTO_2601 372 X 2.1.2.2.1 PSPTO_2145 PvdS 373 X 2.1.2.2.1 PSPTO_3157 Fur 374 X 2.1.2.2.1 PSPTO_2156 PvdS pvdM375 X 2.1.2.2.1 PSPTO_2154 PvdS pvdO376 X 2.1.2.2.1 PSPTO_2133 Fur pvdS377 X 2.1.2.2.1 PSPTO_2604 378 X 2.1.2.2.1 PSPTO_2142 PvdS 379 X 2.1.2.2.1 PSPTO_2600 irp1 380 X 2.1.2.2.1 PSPTO_2139 PvdS 381 X 2.1.2.2.1 PSPTO_2605 Fur 382 X 2.1.2.2.1 PSPTO_5433 383 X 2.1.2.2.1 PSPTO_2602 irp2384 2.1.2.2.2 PSPTO_0912 385 2.1.2.2.2 PSPTO_5087 mdcA 386 2.1.1.1.1.2 PSPTO_2049

Page 219: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

Putative Function phosphoenolpyruvate-protein phosphotransferase,EI HPr EIIA components 1-phosphofructokinase type III effector HopR1 catalase peroxidase HPI hypothetical protein type III secretion protein HrpJ type III effector HopO1-1 negative regulator of hrp expression HrpV type III secretion protein HrpT type III secretion protein HrcQb type III effector HopAJ1 type III effector HopQ1-1 type III secretion cytoplasmic ATPase HrcN type III secretion protein HrcV type III effector HopD1 type III effector HopAK1 type III secretion protein HrpQ type III effector HopAB2 type III chaperone ShcS1 bacterioferritin type III transcriptional regulator HrpS catalase type III effector HopH1 peptidase, M20 M25 M40 family type III effector HopAF1 bacterioferritin RNA polymerase sigma factor HrpL type III secretion protein HrpP type III chaperone ShcO1 type III effector HopK1 type III effector HopAQ1 DNA-binding response regulator CorR type III effector HopM1 type III chaperone protein ShcFtype III chpaerone protein ShcN outer-membrane type III secretion protein HrcC phosphoesterase family protein hypothetical protein type III chaperone ShcM type III effector HopI1 type III secretion protein HrcR type III effector HopX1 type III effector HopAA1-2 type III helper protein HrpK1 type III chaperone ShcS2 conserved effector locus protein carbonic anhydrase type III effector HopY1 type III secretion protein HrpE membrane-bound lytic murein transglycosylase D, putative type III effector HopC1 type III secretion protein HrcQa DNA-binding response regulator type III effector HopN1 DNA-binding response regulator, LuxR family ParA family protein

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses sorted based on their order in the clustering analysis seen in Figure 5A. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3.

Page 220: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

type III effector HopAA1-1 response regulator moxR protein, putative type III effector HopB1 type III helper protein HopP1 type III effector protein AvrE1 type III effector HopS2 carbonic anhydrase type III effector HopG1 hypothetical protein hypothetical protein sulfate transporter family protein HAD-superfamily hydrolase type III transcriptional regulator HrpR type III secretion protein HrpG superoxide dismutase, Fe hypothetical protein type III secretion protein HrpF hypothetical protein quinolinate synthetase type III effector HopS1 type III secretion protein HrpB(Pto) type III secretion protein HrcJ type III secretion protein HrpO protocatechuate 3,4-dioxygenase, alpha subunit type III effector HopT1-1 lipoprotein, putative thiamine biosynthesis lipoprotein, putative type III effector HopE1 enoyl-CoA hydratase type III effector HopA1 type III secretion protein HrpD sensor histidine kinase hypothetical protein cyanide-insensitive terminal oxidase CioB S-adenosylmethionine decarboxylase proenzyme hypothetical protein sulfatase family protein succinate dehydrogenase catalytic subunit 3-methyl-2-oxobutanoate hydroxymethyltransferase adenylate kinase PSPTO_5620 hypothetical protein isoleucyl-tRNA synthetase succinate dehydrogenase, cytochrome b556 subunit dipeptide ABC transporter, permease protein vanillate O-demethylase, oxygenase subunit ATP synthase subunit E cyanide-insensitive terminal oxidase CioA succinate dehydrogenase, hydrophobic membrane anchor protein acetyl-CoA carboxylase beta subunit type III chaperone protein ShcA rubredoxin hypothetical protein 3-deoxy-7-phosphoheptulonate synthase toluene tolerance protein, putative 3-oxoacyl-(acyl carrier protein) synthase protocatechuate 3,4-dioxygenase, beta subunit

Page 221: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

phosphoadenosine phosphosulfate reductase hypothetical protein hypothetical protein hypothetical protein hypothetical protein isocitrate lyase alcohol dehydrogenase, zinc-containing hypothetical protein hypothetical protein ribD C-terminal domain protein major facilitator family transporter nikkomycin biosynthesis domain protein membrane protein, TerC family glucokinase heat shock protein HtpX outer membrane protein OmpW amino acid ABC transporter, ATP-binding protein glycerol kinase DNA-binding protein SpoVR like family protein indole-3-glycerol-phosphate synthase tellurium resistance protein TerZ dienelactone hydrolase family protein cold shock domain family protein PSPTO_5621; csrA-like resolvase, putative aromatic amino acid permease coronafacic acid polyketide synthetase II hypothetical protein hypothetical protein PSPTO_5622 ethanolamine ammonia-lyase, heavy subunit partion protein, ParB family coronafacic acid synthetase, ligase component type III helper protein HrpZ1 amino acid ABC transporter, permease protein CFA synthetase, thioesterase component alcohol dehydrogenase, zinc-containing type III chaperone ShcV glucose-6-phosphate isomerase TonB-dependent receptor, putative glutathione S-transferase family protein amidinotransferase family protein hypothetical protein porin D hypothetical protein hypothetical protein TonB-dependent receptor, putative hypothetical protein transcriptional regulator, AraC family hypothetical protein heat shock protein 90 alcohol dehydrogenase II porin B hypothetical protein fumarate hydratase, class I, putative coronafacic acid polyketide synthase I oxidoreductase, FAD FMN-binding

Page 222: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

xylulokinase cob(I)yrinic acid a,c-diamide adenosyltransferase succinate-semialdehyde dehydrogenase DNA repair protein RecN hypothetical protein phosphate ABC transporter, periplasmic phosphate-binding protein L-arabinose ABC transporter, periplasmic L-arabinose-binding protein hypothetical protein hypothetical protein phosphatidylserine decarboxylase oxidoreductase, molybdopterin-binding ATPase, ParA family type III effector HopV1 glyoxalase, putative recombinase A type III effector HopAD1 membrane protein glyceraldehyde-3-phosphate dehydrogenase hypothetical protein hypothetical protein transcriptional regulator PrtN, putative hypothetical protein indoleacetate-lysine ligase phosphogluconate dehydratase type III helper protein HrpW1 DNA-binding response regulator OmpR DNA-binding response regulator hypothetical protein autotransporting lipase, GDSL family hypothetical protein fumarylacetoacetase aldehyde dehydrogenase family protein iolH protein iolD protein hypothetical protein keto-hydroxyglutarate-aldolase keto-deoxy- phosphogluconate aldolase tellurium resistance protein TerD hypothetical protein methyl-accepting chemotaxis protein polyhydroxyalkanoate granule-associated protein PhaF 6-phosphogluconolactonase lipoprotein, putative glucose-6-phosphate 1-dehydrogenase RNA polymerase sigma factor gas vesicle protein, putative homogentisate 1,2-dioxygenase mannitol ABC transporter, periplasmic mannitol-binding protein ATP-dependent clp protease, ATP-binding subunit ClpA 4-hydroxyphenylpyruvate dioxygenase dnaK suppressor protein, putative hypothetical protein NADH pyrophosphatase hypothetical protein exodeoxyribonuclease V, gamma subunit hypothetical protein 3-oxoacid CoA-transferase, subunit A family outer membrane porin, OprD family bacterial extracellular solute-binding protein, family 5

Page 223: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

acyl-CoA synthase hypothetical protein oxidoreductase, aldo keto reductase family hypothetical protein cyanate hydratase 3-ketoacyl-(acyl-carrier-protein) reductase peptide ABC transporter, periplasmic peptide-binding protein deoxyguanosinetriphosphate triphosphohydrolase carbonic anhydrase aldehyde dehydrogenase family protein nitrogen regulatory protein P-II major facilitator family transporter dicarboxylic acid transport protein type IV pilus biogenesis protein von Willebrand factor type A domain protein high-affinity branched-chain amino acid ABC transporter, periplasmic amino acid-binding protein hypothetical protein mannitol ABC transporter, permease protein thiol peroxidase dipeptide ABC transporter, periplasmic dipeptide-binding protein, putative ATP-dependent protease ATP-binding subunit glutaredoxin triosephosphate isomerase methylenetetrahydrofolate dehydrogenase methenyltetrahydrofolate cyclohydrolase hypothetical protein ABC transporter, ATP-binding protein UDP-N-acetylmuramate--L-alanine ligase aspartyl glutamyl-tRNA amidotransferase subunit C hypothetical protein translation initiation factor IF-1 3-hydroxydecanoyl-ACP dehydratase putative intracellular septation protein stringent starvation protein B peptidyl-tRNA hydrolase hypothetical protein allophanate hydrolase, putative hypothetical protein biotin carboxylase biotin carboxyl carrier protein hypothetical protein hypothetical protein toluene tolerance protein, putative hypothetical protein recombination protein F diadenosinetetraphosphatase hypothetical protein oxidoreductase, aldo keto reductase family ompA family protein hypothetical protein asparagine synthetase, glutamine-hydrolyzing membrane protein TctA, putative membrane protein TctB, putative hypothetical protein TctC protein, putative citrate transporter hypothetical protein lipoprotein, putative acetyltransferase, GNAT family dihydrodipicolinate reductase

Page 224: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

osmotically inducible protein hypothetical protein translation initiation factor IF-3 tRNA (guanine-N(1)-)-methyltransferase hypothetical protein hypothetical protein amino acid ABC transporter, periplasmic amino acid-binding protein 30S ribosomal protein S13 DNA-directed RNA polymerase alpha subunit glycine betaine carnitine choline ABC transporter, permease protein hypothetical protein hypothetical protein 30S ribosomal protein S11 L-lysine 6-monooxygenase translocation protein TolB precursor metal ion transporter, putative 50S ribosomal protein L36 multicopper oxidase outer membrane protein OmpH, putative RNA polymerase sigma-70 factor lipopolysaccharide biosynthesis protein, putative 4-hydroxythreonine-4-phosphate dehydrogenase hypothetical protein 50S ribosomal protein L35 50S ribosomal protein L20 30S ribosomal protein S21 50S ribosomal protein L24 50S ribosomal protein L5 tolA protein 30S ribosomal protein S12 cell division protein FtsK helicase SNF2 family domain protein UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase 50S ribosomal protein L23within intergenic region 6038188-6038782 ribonuclease P hypothetical protein tRNA delta(2)-isopentenylpyrophosphate transferase hypothetical protein 50S ribosomal protein L11 cytidylate kinase phosphoribosyl-ATP pyrophosphatase sulfate ABC transporter, permease protein CysT 50S ribosomal protein L18 hypothetical protein 30S ribosomal protein S6 RNA polymerase sigma-70 factor lipoprotein, putative lipoprotein, putative glutamine synthetase amino acid ABC transporter, periplasmic amino acid-binding protein cold shock protein CapBwithin intergenic region 3679906-3680084 peptidase, M16 family iron-regulated protein A, putativewithin intergenic region 3549362-3549773 Cof-like hydrolase family protein hypothetical protein

Page 225: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

bacterioferritin-associated ferredoxin TonB-dependent siderophore receptor, putative dyp-type peroxidase family protein TonB-dependent siderophore receptor, putative TonB system transport protein ExbD tonB protein TonB-dependent siderophore receptor, putative hypothetical protein 6-phosphogluconate dehydrogenase TonB system transport protein ExbB lipoprotein, putative iron ABC transporter, periplasmic iron-binding protein iron(III) dicitrate transport system, periplasmic iron-binding protein FecB glucose-6-phosphate 1-dehydrogenase MbtH-like protein cation ABC transporter, periplasmic cation-binding protein aminotransferase, class V yersiniabactin synthetase, salycilate ligase component ABC transporter, ATP-binding permease protein pyoverdine sidechain peptide synthetase II, D-Asp-L-Thr component pyoverdine biosynthesis regulatory gene, putative pyoverdine synthetase, thioesterase component TonB-dependent siderophore receptor yersiniabactin synthetase, thioesterase component hypothetical protein iron-regulated membrane protein, putative hypothetical protein renal dipeptidase family protein hypothetical protein RNA polymerase sigma-70 factor ABC transporter, ATP-binding permease protein hypothetical protein yersiniabactin polyketide non-ribosomal peptide synthetase cation ABC transporter, permease protein TonB-dependent siderophore receptor, putative hypothetical protein yersiniabactin non-ribosomal peptide synthetase methyl-accepting chemotaxis protein malonate decarboxylase, alpha subunit hypothetical protein

Page 226: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses sorted based on their order in the clustering analysis seen in Figure 5A. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3.

Page 227: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 228: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 229: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 230: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 231: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 232: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 233: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III

: Differentially regulated genes identified at a p value less than or equal to 0.01 using a GCRMA/FDR analyses sorted based on their order in the clustering analysis seen in Figure 5A. Columns D through K correspond to comparisons between different time points/conditions as described in Figure 3.

Page 234: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 235: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 236: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 237: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 238: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III
Page 239: 12866_2008_642_MOESM1_ESM.xls… · XLS file · Web view · 2015-12-11plays a role in assembling DnaB onto the primer template and interacts with the core polymerase ... type III