|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
283-743 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 839.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 283 LLNDPISRDNQ-DQIWVREQQELLEKTLKHFNVRAKVVNATQGPAVTRFEVQPEIGVKVSKVKNLSDDLKLNMAARDIRI 361
Cdd:COG1674 142 LLDPPPPKKEKiDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 362 EAPIPGKNTIGIEIPNQTSQTVGLQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNIQKMPHGLIAGATGSGKSVCINTI 441
Cdd:COG1674 222 EAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAM 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 442 LISLLYKASHEDVKFLLIDPKMVELAPFNEIPHLVSPVITDVKAATIALKWAVNEMEERYEKFVHEGVRDIERFNQKVIK 521
Cdd:COG1674 302 ILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVRE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 522 ------QGRSDEKMPFLVIVIDELADLMMAAPQDVEDSICRIAQKARACGMHLLVATQRPSVDVITGLIKANIPTRIAFS 595
Cdd:COG1674 382 akakgeEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 596 VSSQVDSRTIIDTNGAEKLLGKGDMLFVENGSGKSVRLQGAFVSDDEIERVTRHIRSIAPPDYL--FEQEQLLEQVMVDE 673
Cdd:COG1674 462 VSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIeeILEEEEEEDEGGDD 541
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 674 EDEDDLLSDAIKFVMKQNGASTSLLQRHFKIGYNRAARLMDTMEMRGIISEQNGSKPREILLSTQQLEAM 743
Cdd:COG1674 542 DEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
99-734 |
3.44e-147 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 464.17 E-value: 3.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 99 EPTRERKKQVKQDRGPFQPTQVASPIHGYQQQKKdqevenvPAFIRKQHEEEvkedstaEKPVSIEPEVTEtvPEKPVAV 178
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQ-------PVAPQPQYQQP-------QQPVAPQPQYQQ--PQQPVAP 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 179 DDEQAKTEEVIQDKPsQMEKVTKPSEPkkrmkdkkkrnpitnntKQQGSLPFNVMMSSNDKRKQEireklsavrpvkpvk 258
Cdd:PRK10263 814 QPQYQQPQQPVAPQP-QYQQPQQPVAP-----------------QPQDTLLHPLLMRNGDSRPLH--------------- 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 259 pvkpaetvKPEQPKPKRSFEVPNYLLNDPIsrdnqDQIWVREQQELLEKTLKHFNVRAKVVNATQGPAVTRFEVQPEIGV 338
Cdd:PRK10263 861 --------KPTTPLPSLDLLTPPPSEVEPV-----DTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGV 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 339 KVSKVKNLSDDLKLNMAARDIRIEAPIPGKNTIGIEIPNQTSQTVGLQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNI 418
Cdd:PRK10263 928 KAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADL 1007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 419 QKMPHGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKMVELAPFNEIPHLVSPVITDVKAATIALKWAVNEME 498
Cdd:PRK10263 1008 AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEME 1087
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 499 ERYEKFVHEGVRDIERFNQKVIKQGRSD---------------------EKMPFLVIVIDELADLMMAAPQDVEDSICRI 557
Cdd:PRK10263 1088 RRYKLMSALGVRNLAGYNEKIAEADRMMrpipdpywkpgdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARL 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 558 AQKARACGMHLLVATQRPSVDVITGLIKANIPTRIAFSVSSQVDSRTIIDTNGAEKLLGKGDMLFVENGSGKSVRLQGAF 637
Cdd:PRK10263 1168 AQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAF 1247
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 638 VSDDEIERVTRHIRSIAPPDYlfeqeqlLEQVMVDEEDE------------DDLLSDAIKFVMKQNGASTSLLQRHFKIG 705
Cdd:PRK10263 1248 VRDQEVHAVVQDWKARGRPQY-------VDGITSDSESEggaggfdgaeelDPLFDQAVQFVTEKRKASISGVQRQFRIG 1320
|
650 660
....*....|....*....|....*....
gi 1219746731 706 YNRAARLMDTMEMRGIISEQNGSKPREIL 734
Cdd:PRK10263 1321 YNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
385-576 |
4.43e-72 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 233.81 E-value: 4.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 385 LQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNIQKMP-HGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKM 463
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 464 VELAPFNEIPHLVS-PVITDVKAATIALKWAVNEMEERYEKFVHEGVRDIERFNQKV---------------------IK 521
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1219746731 522 QGRSDEKMPFLVIVIDELADLMMAAPQD----VEDSICRIAQKARACGMHLLVATQRPS 576
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
674-736 |
1.09e-27 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 105.96 E-value: 1.09e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219746731 674 EDEDDLLSDAIKFVMKQNGASTSLLQRHFKIGYNRAARLMDTMEMRGIISEQNGSKPREILLS 736
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
401-641 |
3.79e-26 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 114.30 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 401 LTVGLGLNIEGTPMVTNI-----QKM-PHGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKM-VELAPFNEIP 473
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLkesaeGGMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGgATFLGLEGLP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 474 HlVSPVITDV--KAATIA-LKWAVN-EMEERYEKFVHEG-VRDIERFNQkVIKQGRSDEKMPFLVIVIDELADLMMAAPQ 548
Cdd:TIGR03924 489 H-VSAVITNLadEAPLVDrMQDALAgEMNRRQELLRAAGnFANVAEYEK-ARAAGADLPPLPALFVVVDEFSELLSQHPD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 549 --DVEDSICRIaqkARACGMHLLVATQRPSVDVITGLiKANIPTRIAFSVSSQVDSRTIIDTNGAEKLLGKGDMLFVENG 626
Cdd:TIGR03924 567 faDLFVAIGRL---GRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVD 642
|
250
....*....|....*
gi 1219746731 627 SGKSVRLQGAFVSDD 641
Cdd:TIGR03924 643 TAEPVRFRAAYVSGP 657
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
59-205 |
7.02e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.02 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 59 DRGEQSKPMD--TPAYQRRSSDDYKREQRIQ----------------KKSKPTNEQRHEPTRERKKQVKQDRGPFQPTQV 120
Cdd:PRK10811 616 DRNERRDTRDnrTRREGRENREENRRNRRQAqqqtaetresqqaevtEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAK 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 121 ASPIHGYQQQKKDQEVENVPAFIRKQH---EEEVKEDStAEKPVSIEPEVTETVPEKPVAVDDEQAKTEEVIQDKPSQME 197
Cdd:PRK10811 696 ALNVEEQSVQETEQEERVQQVQPRRKQrqlNQKVRIEQ-SVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQ 774
|
....*...
gi 1219746731 198 KVTKPSEP 205
Cdd:PRK10811 775 TAPEQDEE 782
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
283-743 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 839.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 283 LLNDPISRDNQ-DQIWVREQQELLEKTLKHFNVRAKVVNATQGPAVTRFEVQPEIGVKVSKVKNLSDDLKLNMAARDIRI 361
Cdd:COG1674 142 LLDPPPPKKEKiDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 362 EAPIPGKNTIGIEIPNQTSQTVGLQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNIQKMPHGLIAGATGSGKSVCINTI 441
Cdd:COG1674 222 EAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAM 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 442 LISLLYKASHEDVKFLLIDPKMVELAPFNEIPHLVSPVITDVKAATIALKWAVNEMEERYEKFVHEGVRDIERFNQKVIK 521
Cdd:COG1674 302 ILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVRE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 522 ------QGRSDEKMPFLVIVIDELADLMMAAPQDVEDSICRIAQKARACGMHLLVATQRPSVDVITGLIKANIPTRIAFS 595
Cdd:COG1674 382 akakgeEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 596 VSSQVDSRTIIDTNGAEKLLGKGDMLFVENGSGKSVRLQGAFVSDDEIERVTRHIRSIAPPDYL--FEQEQLLEQVMVDE 673
Cdd:COG1674 462 VSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIeeILEEEEEEDEGGDD 541
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 674 EDEDDLLSDAIKFVMKQNGASTSLLQRHFKIGYNRAARLMDTMEMRGIISEQNGSKPREILLSTQQLEAM 743
Cdd:COG1674 542 DEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
99-734 |
3.44e-147 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 464.17 E-value: 3.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 99 EPTRERKKQVKQDRGPFQPTQVASPIHGYQQQKKdqevenvPAFIRKQHEEEvkedstaEKPVSIEPEVTEtvPEKPVAV 178
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQ-------PVAPQPQYQQP-------QQPVAPQPQYQQ--PQQPVAP 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 179 DDEQAKTEEVIQDKPsQMEKVTKPSEPkkrmkdkkkrnpitnntKQQGSLPFNVMMSSNDKRKQEireklsavrpvkpvk 258
Cdd:PRK10263 814 QPQYQQPQQPVAPQP-QYQQPQQPVAP-----------------QPQDTLLHPLLMRNGDSRPLH--------------- 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 259 pvkpaetvKPEQPKPKRSFEVPNYLLNDPIsrdnqDQIWVREQQELLEKTLKHFNVRAKVVNATQGPAVTRFEVQPEIGV 338
Cdd:PRK10263 861 --------KPTTPLPSLDLLTPPPSEVEPV-----DTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGV 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 339 KVSKVKNLSDDLKLNMAARDIRIEAPIPGKNTIGIEIPNQTSQTVGLQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNI 418
Cdd:PRK10263 928 KAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADL 1007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 419 QKMPHGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKMVELAPFNEIPHLVSPVITDVKAATIALKWAVNEME 498
Cdd:PRK10263 1008 AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEME 1087
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 499 ERYEKFVHEGVRDIERFNQKVIKQGRSD---------------------EKMPFLVIVIDELADLMMAAPQDVEDSICRI 557
Cdd:PRK10263 1088 RRYKLMSALGVRNLAGYNEKIAEADRMMrpipdpywkpgdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARL 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 558 AQKARACGMHLLVATQRPSVDVITGLIKANIPTRIAFSVSSQVDSRTIIDTNGAEKLLGKGDMLFVENGSGKSVRLQGAF 637
Cdd:PRK10263 1168 AQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAF 1247
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 638 VSDDEIERVTRHIRSIAPPDYlfeqeqlLEQVMVDEEDE------------DDLLSDAIKFVMKQNGASTSLLQRHFKIG 705
Cdd:PRK10263 1248 VRDQEVHAVVQDWKARGRPQY-------VDGITSDSESEggaggfdgaeelDPLFDQAVQFVTEKRKASISGVQRQFRIG 1320
|
650 660
....*....|....*....|....*....
gi 1219746731 706 YNRAARLMDTMEMRGIISEQNGSKPREIL 734
Cdd:PRK10263 1321 YNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
385-576 |
4.43e-72 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 233.81 E-value: 4.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 385 LQEIFETSAFQGSSSPLTVGLGLNIEGTPMVTNIQKMP-HGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKM 463
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 464 VELAPFNEIPHLVS-PVITDVKAATIALKWAVNEMEERYEKFVHEGVRDIERFNQKV---------------------IK 521
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1219746731 522 QGRSDEKMPFLVIVIDELADLMMAAPQD----VEDSICRIAQKARACGMHLLVATQRPS 576
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
283-377 |
7.96e-39 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 138.82 E-value: 7.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 283 LLNDPISRDNQDQIWVREQQELLEKTLKHFNVRAKVVNATQGPAVTRFEVQPEIGVKVSKVKNLSDDLKLNMAARDIRIE 362
Cdd:pfam17854 7 LEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAPSIRIV 86
|
90
....*....|....*
gi 1219746731 363 APIPGKNTIGIEIPN 377
Cdd:pfam17854 87 APIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
674-736 |
6.45e-31 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 115.16 E-value: 6.45e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219746731 674 EDEDDLLSDAIKFVMKQNGASTSLLQRHFKIGYNRAARLMDTMEMRGIISEQNGSKPREILLS 736
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
674-736 |
1.09e-27 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 105.96 E-value: 1.09e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1219746731 674 EDEDDLLSDAIKFVMKQNGASTSLLQRHFKIGYNRAARLMDTMEMRGIISEQNGSKPREILLS 736
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
401-641 |
3.79e-26 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 114.30 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 401 LTVGLGLNIEGTPMVTNI-----QKM-PHGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKM-VELAPFNEIP 473
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLkesaeGGMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGgATFLGLEGLP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 474 HlVSPVITDV--KAATIA-LKWAVN-EMEERYEKFVHEG-VRDIERFNQkVIKQGRSDEKMPFLVIVIDELADLMMAAPQ 548
Cdd:TIGR03924 489 H-VSAVITNLadEAPLVDrMQDALAgEMNRRQELLRAAGnFANVAEYEK-ARAAGADLPPLPALFVVVDEFSELLSQHPD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 549 --DVEDSICRIaqkARACGMHLLVATQRPSVDVITGLiKANIPTRIAFSVSSQVDSRTIIDTNGAEKLLGKGDMLFVENG 626
Cdd:TIGR03924 567 faDLFVAIGRL---GRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVD 642
|
250
....*....|....*
gi 1219746731 627 SGKSVRLQGAFVSDD 641
Cdd:TIGR03924 643 TAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
296-611 |
5.87e-26 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 114.70 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 296 IWVREQQELLEKtlkHFNVRAKVVNATQGPAVTRFEVQPEIGVKVSKVknlsDDLKLNMAARDIrieAPIPGKNTIGIEI 375
Cdd:TIGR03928 344 IFVQDVMESLPE---NVKTVIDIKNRNEGEIVLEEGELVEKSFTPDHL----DNEDLEEYSRTL---APLNHLQNLKNSI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 376 PNQTS----------QTVGLQEIFETSAfqgSSSPLTVGLGLNIEGTPMVTNI-QKM--PHGLIAGATGSGKSVCINTIL 442
Cdd:TIGR03928 414 PESVTflemygvkkvEELNIQERWAKNE---TYKSLAVPIGLRGKDDIVYLNLhEKAhgPHGLVAGTTGSGKSEILQTYI 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 443 ISLLYKASHEDVKFLLIDPKMVELA-PFNEIPHLVSpVITDVKAATI--ALKWAVNEMEERYEKFVHEGVRDIERFnQKV 519
Cdd:TIGR03928 491 LSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITNLDGAQSmrALASIKAELKKRQRLFGENNVNHINQY-QKL 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 520 IKQGRSDEKMPFLVIVIDELADLMMAAPqDVEDSICRIAQKARACGMHLLVATQRPSvDVITGLIKANIPTRIAFSVSSQ 599
Cdd:TIGR03928 569 YKQGKAKEPMPHLFLISDEFAELKSEQP-EFMKELVSTARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDA 646
|
330
....*....|..
gi 1219746731 600 VDSRTIIDTNGA 611
Cdd:TIGR03928 647 SDSNEILKTPDA 658
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
412-606 |
3.17e-16 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 83.50 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 412 TPMVTNIQKMPHGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKMVELAPFNEIPHlVSPVIT--DVKAATIA 489
Cdd:TIGR03928 801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 490 LKWAVNEMEERYEKFVHEGVRDIERFNQKvikqgrSDEKMPFLVIVIDELaDLMMAAP--QDVEDSICRIAQKARACGMH 567
Cdd:TIGR03928 880 IRRIKKEIDRRKKLFSEYGVASISMYNKA------SGEKLPQIVIIIDNY-DAVKEEPfyEDFEELLIQLAREGASLGIY 952
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1219746731 568 LLV-ATQRPSVDVItglIKANIPTRIAFSVSSQVDSRTII 606
Cdd:TIGR03928 953 LVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
390-634 |
1.81e-09 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 60.39 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 390 ETSAFQGSSSPLTVGLGLNiEGTPMVTNIQKM--PHGLIAGATGSGKSvciNTILIsLLYKASHEDVKFLLIDPK----- 462
Cdd:COG0433 15 ELEELLGDGGGILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKS---NTLQV-LLEELSRAGVPVLVFDPHgeysg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 463 -----------------MVELAPFN-----------------------------------------------------EI 472
Cdd:COG0433 90 laepgaeradvgvfdpgAGRPLPINpwdlfataselgplllsrldlndtqrgvlrealrladdkglllldlkdliallEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 473 PHLVSPVITDVKAATI-ALKWAVNEMEERYEKFVHEGVR--------------DIERFNQKV----------------IK 521
Cdd:COG0433 170 GEELGEEYGNVSAASAgALLRRLESLESADGLFGEPGLDledllrtdgrvtviDLSGLPEELqstfvlwllrelfearPE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 522 QGRSDEKMPFLVIVIDELADLMMAAPQDVEDSICRIAQKARACGMHLLVATQRPSvDVITGlIKANIPTRIAFSVSSQVD 601
Cdd:COG0433 250 VGDADDRKLPLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRD 327
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1219746731 602 SRTI------IDTNGAEKL--LGKGDMLFVENGSGKSVRLQ 634
Cdd:COG0433 328 QKAVkaaaetLSEDLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
385-633 |
6.54e-08 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 56.53 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 385 LQEIFETSAFQGSSSPLTVGLGLNIEG-TPMVTNIQKMPHGLIAGATGSGKSVCINTILISLLYKashEDVKFLLIDPKM 463
Cdd:TIGR03928 1059 LEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSID 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 464 VELAPFNEIPHLVSpVITDVKAATIALKWAVNEMEERYEKFVHEGVRDIERFNQKVIkqgrsdekmpflVIVIDELADLM 543
Cdd:TIGR03928 1136 RGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELREAAYKEALQNETGEPAFKPI------------LLIIDDLEDFI 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 544 MAAPQDVEDSICRIAQKARACGMHLLVATQRPSV----DVITGLIKAnipTRIAFSVSSQVDSRTI-IDTNGAEKLLGKG 618
Cdd:TIGR03928 1203 QRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPG 1279
|
250
....*....|....*
gi 1219746731 619 DMLFVENGSGKSVRL 633
Cdd:TIGR03928 1280 EGYFVVNGKYQKIKI 1294
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
423-603 |
2.14e-07 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 54.23 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 423 HGLIAGATGSGKSVCINTILISLLYKASHEDVKFLLIDPKMVELAPFNEIPH---LVSPVITDVKAATIALKWAVneMEE 499
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHvggVAGRLDPERVRRTVAEVEGL--LRR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 500 RYEKFVHEGVRDIERFNQKVIKQGRSDEKMPFLVIVIDELADLmMAAPQDVEDSICRIAQKARACGMHLLVATQRPSvdV 579
Cdd:TIGR03925 159 RERLFRTHGIDSMAQYRARRAAGRLPEDPFGDVFLVIDGWGTL-RQDFEDLEDKVTDLAARGLAYGVHVVLTASRWS--E 235
|
170 180
....*....|....*....|....*...
gi 1219746731 580 ITGLIKANIPTRIAF----SVSSQVDSR 603
Cdd:TIGR03925 236 IRPALRDLIGTRIELrlgdPMDSEIDRR 263
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
391-461 |
2.23e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.47 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1219746731 391 TSAFQGSSSPLTVGLGLNieGTPMVTNI---QKMPHGLIAGATGSGKSVCINTILISLLYKasheDVKFLLIDP 461
Cdd:COG3451 173 HSFELGDPWGIYLLNTRS--GTPVFFDFhdgLDNGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
59-205 |
7.02e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.02 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 59 DRGEQSKPMD--TPAYQRRSSDDYKREQRIQ----------------KKSKPTNEQRHEPTRERKKQVKQDRGPFQPTQV 120
Cdd:PRK10811 616 DRNERRDTRDnrTRREGRENREENRRNRRQAqqqtaetresqqaevtEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAK 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219746731 121 ASPIHGYQQQKKDQEVENVPAFIRKQH---EEEVKEDStAEKPVSIEPEVTETVPEKPVAVDDEQAKTEEVIQDKPSQME 197
Cdd:PRK10811 696 ALNVEEQSVQETEQEERVQQVQPRRKQrqlNQKVRIEQ-SVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQ 774
|
....*...
gi 1219746731 198 KVTKPSEP 205
Cdd:PRK10811 775 TAPEQDEE 782
|
|
| |
