|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
340-835 |
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: 798.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 340 AAPATTRLVPRGEQGELENSRPYILPSNDILAHGAP--HKTRSAANDRVVDALKQVLEDFGVNAEVTGFTRGPTVTRYEL 417
Cdd:COG1674 113 LAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 418 ELGQGVKVERITNLSKNIAYAVASPDVRILSPIPGKSAIGIEIPNVDRETVALGDVLRSSTAMKNDHPMAIGIGKDVEGG 497
Cdd:COG1674 193 EPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 498 YVMANLAKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHLITPIITDPKKAAQALEW 577
Cdd:COG1674 273 PVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKW 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 578 VVKEMDMRYDDLALFGFKHIDDFNKAVRSGKVKPLPgsERTLTTYPYLLVIVDELADLMMVAPRDVDESIQRITQLARAA 657
Cdd:COG1674 353 AVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGEE--EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 658 GIHLVLATQRPSVDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDALFLPMGESKPMRVQGSWVSETEIH 737
Cdd:COG1674 431 GIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 738 AAVDHAKEQANPEYREDVTQAQSSAVVAEDIGDDLDDLIAAAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIV 817
Cdd:COG1674 511 RVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....*...
gi 2724155046 818 GPSQGSKARDVLVSPDEL 835
Cdd:COG1674 591 GPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
364-832 |
1.27e-122 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 402.16 E-value: 1.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 364 LPSNDILahgaphkTRSAANDRVVD--ALKQV-------LEDFGVNAEVTGFTRGPTVTRYELELGQGVKVERITNLSKN 434
Cdd:PRK10263 866 LPSLDLL-------TPPPSEVEPVDtfALEQMarlvearLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRD 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 435 IAYAVASPDVRILSPIPGKSAIGIEIPNVDRETVALGDVLRSSTAMKNDHPMAIGIGKDVEGGYVMANLAKMPHMLVAGA 514
Cdd:PRK10263 939 LARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGT 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 515 TGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHLITPIITDPKKAAQALEWVVKEMDMRYDDLALFGF 594
Cdd:PRK10263 1019 TGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGV 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 595 KHIDDFN----KAVRSGKVKPLP---------GSERTLTTYPYLLVIVDELADLMMVAPRDVDESIQRITQLARAAGIHL 661
Cdd:PRK10263 1099 RNLAGYNekiaEADRMMRPIPDPywkpgdsmdAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHL 1178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 662 VLATQRPSVDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDALFLPMGESKPMRVQGSWVSETEIHAAVD 741
Cdd:PRK10263 1179 VLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQ 1258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 742 HAKEQANPEYREDVT---QAQSSAVVAEDIGDDLDDLIAAAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIVG 818
Cdd:PRK10263 1259 DWKARGRPQYVDGITsdsESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVS 1338
|
490
....*....|....
gi 2724155046 819 PSQGSKARDVLVSP 832
Cdd:PRK10263 1339 EQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
470-669 |
1.76e-57 |
|
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: 196.44 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 470 LGDVLRSSTAMKNDHPMAIGIGKDVEGGYVMANLAKMP-HMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKR 548
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 549 VELTIYEGIPHLIT-PIITDPKKAAQALEWVVKEMDMRYDDLALFGFKHIDDFNK-------------AVRSGKVKPLPG 614
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGeiaedpldgfgdvFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2724155046 615 SERTLTTYPYLLVIVDELADLMMVAPRD----VDESIQRITQLARAAGIHLVLATQRPS 669
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
488-713 |
2.96e-23 |
|
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: 106.61 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 488 IGI-GKDvegGYVMANL---AKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELT-IYEGIPHL-- 560
Cdd:TIGR03928 450 IGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLlg 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 561 -ITPIitDPKKAAQALEWVVKEMDMRYDDLALFGFKHIDDFNKAVRSGKVK-PLpgsertlttyPYLLVIVDELADLMMV 638
Cdd:TIGR03928 527 tITNL--DGAQSMRALASIKAELKKRQRLFGENNVNHINQYQKLYKQGKAKePM----------PHLFLISDEFAELKSE 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2724155046 639 APRDVDE--SIQRItqlARAAGIHLVLATQRPSvDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDA 713
Cdd:TIGR03928 595 QPEFMKElvSTARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRA 667
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
778-831 |
8.86e-20 |
|
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: 83.62 E-value: 8.86e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2724155046 778 AAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIVGPSQGSKARDVLVS 831
Cdd:smart00843 10 AVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
508-689 |
3.13e-10 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 59.16 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 508 HMLVAGATGAGKSSFVNSMITSILMRATpdevRMVLVDPKRvELTIyegiphlitpiitdpkkaaqalewVVKEMDMRYD 587
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG-ELFL------------------------VIPDRDDSFA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 588 DL-ALFgFKHIDDFNKAVRSGKVKPLPgsertlttyPYLLVIVDELADLMMVaprdvdESIQRITQLARAAGIHLVLATQ 666
Cdd:cd01127 52 ALrALF-FNQLFRALTELASLSPGRLP---------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQ 115
|
170 180
....*....|....*....|....*....
gi 2724155046 667 ------RPSVDIITGTIKANVPSRLAFAT 689
Cdd:cd01127 116 slaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
114-221 |
8.51e-10 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 58.75 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 114 LPIVLIAFAVRLFRAPQEEQANHRLsLGAFVLLLTTTGLIAIAEgrPSPTDGLEGlqEAGGLVGWAIGNGLANLLSTPLA 193
Cdd:pfam13491 69 LPVALLYWGWRLFRRRSLERRWLRL-LGFLLLLLASSALFALRL--PSLEFGLPG--GAGGVIGRLLANALVTLLGFTGA 143
|
90 100
....*....|....*....|....*...
gi 2724155046 194 VIVLILVTLLGVLIVVGLPMRELVALIR 221
Cdd:pfam13491 144 TLLLLALLAIGLSLVTGFSWLALAERLG 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
340-835 |
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: 798.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 340 AAPATTRLVPRGEQGELENSRPYILPSNDILAHGAP--HKTRSAANDRVVDALKQVLEDFGVNAEVTGFTRGPTVTRYEL 417
Cdd:COG1674 113 LAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 418 ELGQGVKVERITNLSKNIAYAVASPDVRILSPIPGKSAIGIEIPNVDRETVALGDVLRSSTAMKNDHPMAIGIGKDVEGG 497
Cdd:COG1674 193 EPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 498 YVMANLAKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHLITPIITDPKKAAQALEW 577
Cdd:COG1674 273 PVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKW 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 578 VVKEMDMRYDDLALFGFKHIDDFNKAVRSGKVKPLPgsERTLTTYPYLLVIVDELADLMMVAPRDVDESIQRITQLARAA 657
Cdd:COG1674 353 AVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGEE--EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 658 GIHLVLATQRPSVDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDALFLPMGESKPMRVQGSWVSETEIH 737
Cdd:COG1674 431 GIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 738 AAVDHAKEQANPEYREDVTQAQSSAVVAEDIGDDLDDLIAAAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIV 817
Cdd:COG1674 511 RVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....*...
gi 2724155046 818 GPSQGSKARDVLVSPDEL 835
Cdd:COG1674 591 GPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
364-832 |
1.27e-122 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 402.16 E-value: 1.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 364 LPSNDILahgaphkTRSAANDRVVD--ALKQV-------LEDFGVNAEVTGFTRGPTVTRYELELGQGVKVERITNLSKN 434
Cdd:PRK10263 866 LPSLDLL-------TPPPSEVEPVDtfALEQMarlvearLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRD 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 435 IAYAVASPDVRILSPIPGKSAIGIEIPNVDRETVALGDVLRSSTAMKNDHPMAIGIGKDVEGGYVMANLAKMPHMLVAGA 514
Cdd:PRK10263 939 LARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGT 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 515 TGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHLITPIITDPKKAAQALEWVVKEMDMRYDDLALFGF 594
Cdd:PRK10263 1019 TGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGV 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 595 KHIDDFN----KAVRSGKVKPLP---------GSERTLTTYPYLLVIVDELADLMMVAPRDVDESIQRITQLARAAGIHL 661
Cdd:PRK10263 1099 RNLAGYNekiaEADRMMRPIPDPywkpgdsmdAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHL 1178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 662 VLATQRPSVDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDALFLPMGESKPMRVQGSWVSETEIHAAVD 741
Cdd:PRK10263 1179 VLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQ 1258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 742 HAKEQANPEYREDVT---QAQSSAVVAEDIGDDLDDLIAAAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIVG 818
Cdd:PRK10263 1259 DWKARGRPQYVDGITsdsESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVS 1338
|
490
....*....|....
gi 2724155046 819 PSQGSKARDVLVSP 832
Cdd:PRK10263 1339 EQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
470-669 |
1.76e-57 |
|
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: 196.44 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 470 LGDVLRSSTAMKNDHPMAIGIGKDVEGGYVMANLAKMP-HMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKR 548
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 549 VELTIYEGIPHLIT-PIITDPKKAAQALEWVVKEMDMRYDDLALFGFKHIDDFNK-------------AVRSGKVKPLPG 614
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGeiaedpldgfgdvFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2724155046 615 SERTLTTYPYLLVIVDELADLMMVAPRD----VDESIQRITQLARAAGIHLVLATQRPS 669
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
364-462 |
5.27e-35 |
|
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: 128.42 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 364 LPSNDILAHGAPH--KTRSAANDRVVDALKQVLEDFGVNAEVTGFTRGPTVTRYELELGQGVKVERITNLSKNIAYAVAS 441
Cdd:pfam17854 1 LPPLDLLEPPPTSsqKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 2724155046 442 PDVRILSPIPGKSAIGIEIPN 462
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
488-713 |
2.96e-23 |
|
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: 106.61 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 488 IGI-GKDvegGYVMANL---AKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELT-IYEGIPHL-- 560
Cdd:TIGR03928 450 IGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLlg 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 561 -ITPIitDPKKAAQALEWVVKEMDMRYDDLALFGFKHIDDFNKAVRSGKVK-PLpgsertlttyPYLLVIVDELADLMMV 638
Cdd:TIGR03928 527 tITNL--DGAQSMRALASIKAELKKRQRLFGENNVNHINQYQKLYKQGKAKePM----------PHLFLISDEFAELKSE 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2724155046 639 APRDVDE--SIQRItqlARAAGIHLVLATQRPSvDIITGTIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDA 713
Cdd:TIGR03928 595 QPEFMKElvSTARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRA 667
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
778-831 |
1.06e-21 |
|
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: 88.97 E-value: 1.06e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2724155046 778 AAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIVGPSQGSKARDVLVS 831
Cdd:pfam09397 10 AVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
778-831 |
8.86e-20 |
|
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: 83.62 E-value: 8.86e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2724155046 778 AAELVITTQLGSTSMLQRKLKMGFAKAGRLMDLLESREIVGPSQGSKARDVLVS 831
Cdd:smart00843 10 AVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
507-732 |
2.46e-18 |
|
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: 90.03 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 507 PHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPK-RVELTIYEGIPHlITPIITDpkkAAQALEWVVK----- 580
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKgGATFLGLEGLPH-VSAVITN---LADEAPLVDRmqdal 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 581 --EMDMRYDDL-ALFGFKHIDDFNKAVRSGkvkplpgseRTLTTYPYLLVIVDELADLMMVAPrDVDESIQRITQLARAA 657
Cdd:TIGR03924 512 agEMNRRQELLrAAGNFANVAEYEKARAAG---------ADLPPLPALFVVVDEFSELLSQHP-DFADLFVAIGRLGRSL 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2724155046 658 GIHLVLATQRPSVDIITGtIKANVPSRLAFATSSLADSRVVLDMPGAEKLIGQGDALFLPMGESKPMRVQGSWVS 732
Cdd:TIGR03924 582 GVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVS 655
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
508-689 |
3.13e-10 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 59.16 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 508 HMLVAGATGAGKSSFVNSMITSILMRATpdevRMVLVDPKRvELTIyegiphlitpiitdpkkaaqalewVVKEMDMRYD 587
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG-ELFL------------------------VIPDRDDSFA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 588 DL-ALFgFKHIDDFNKAVRSGKVKPLPgsertlttyPYLLVIVDELADLMMVaprdvdESIQRITQLARAAGIHLVLATQ 666
Cdd:cd01127 52 ALrALF-FNQLFRALTELASLSPGRLP---------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQ 115
|
170 180
....*....|....*....|....*....
gi 2724155046 667 ------RPSVDIITGTIKANVPSRLAFAT 689
Cdd:cd01127 116 slaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
114-221 |
8.51e-10 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 58.75 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 114 LPIVLIAFAVRLFRAPQEEQANHRLsLGAFVLLLTTTGLIAIAEgrPSPTDGLEGlqEAGGLVGWAIGNGLANLLSTPLA 193
Cdd:pfam13491 69 LPVALLYWGWRLFRRRSLERRWLRL-LGFLLLLLASSALFALRL--PSLEFGLPG--GAGGVIGRLLANALVTLLGFTGA 143
|
90 100
....*....|....*....|....*...
gi 2724155046 194 VIVLILVTLLGVLIVVGLPMRELVALIR 221
Cdd:pfam13491 144 TLLLLALLAIGLSLVTGFSWLALAERLG 171
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
502-687 |
3.10e-09 |
|
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: 61.16 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 502 NLAKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHlITPIIT--DPKKAAQALEWVV 579
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLIRRIK 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 580 KEMDMRYDDLALFGFKHIDDFNKAvrsgkvkplpgSERTLttyPYLLVIVDELaDLMMVAPR-DVDESIqrITQLAR--- 655
Cdd:TIGR03928 885 KEIDRRKKLFSEYGVASISMYNKA-----------SGEKL---PQIVIIIDNY-DAVKEEPFyEDFEEL--LIQLARega 947
|
170 180 190
....*....|....*....|....*....|...
gi 2724155046 656 AAGIHLVL-ATQRPSVDIitgTIKANVPSRLAF 687
Cdd:TIGR03928 948 SLGIYLVMtAGRQNAVRM---PLMNNIKTKIAL 977
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
460-726 |
4.62e-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: 57.31 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 460 IPNVdRETVALGDVLRSSTAMKNDHPMAIGIGKDVEG-GYVMANLAKMPHMLVAGATGAGKSSFVNSMITSILMRatpDE 538
Cdd:TIGR03928 1050 IPMV-PEELSLEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EK 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 539 VRMVLVDPKRVELTIYEGIPHLITpIITDPKKAAQALEWVVKEMDMRyddlalfgfkhiddfnkavRSGKVKPLPGSERT 618
Cdd:TIGR03928 1126 EKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELR-------------------EAAYKEALQNETGE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 619 LTTYPYLLVIvDELADLMMVAPRDVDESIQRITQLARAAGIHLVLATQRPSV----DIITGTIKAnvpSRLAFATSSLAD 694
Cdd:TIGR03928 1186 PAFKPILLII-DDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSD 1261
|
250 260 270
....*....|....*....|....*....|...
gi 2724155046 695 SRVV-LDMPGAEKLIGQGDALFLPMGESKPMRV 726
Cdd:TIGR03928 1262 QSFFkLPFTRSEKELEPGEGYFVVNGKYQKIKI 1294
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
483-548 |
6.20e-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: 53.07 E-value: 6.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2724155046 483 DHPMAIGIGkDVEGGYVMANLAKMPHMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKR 548
Cdd:TIGR03925 341 RLRVPLGLG-ESDLAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRR 405
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
507-578 |
2.68e-05 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 47.63 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 507 PHMLVAGATGAGKSSFVNSMITSILMRatpdEVRMVLVDPKR-----VE------LTIYEGIPHLITP--IITDPKKAAQ 573
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDPGGsyeilVRalggtyIDLSPGSPTGLNPfdLEDTEEKRDF 280
|
....*
gi 2724155046 574 ALEWV 578
Cdd:COG3451 281 LLELL 285
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
508-702 |
2.86e-05 |
|
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: 47.68 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 508 HMLVAGATGAGKSSFVNSMITSILMRATPDEVRMVLVDPKRVELTIYEGIPHlITPIIT--DPKKAAQALEWVVKEMDMR 585
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 586 YDDLALFGFKHIDDFNKAVRSGKVKPLPGSErtlttypyLLVIVDELADLMmvapRDVDESIQRITQLAR---AAGIHLV 662
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRLPEDPFGD--------VFLVIDGWGTLR----QDFEDLEDKVTDLAArglAYGVHVV 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2724155046 663 LAT-----QRPSV-DIITGTIKAnvpsRLAFATSSLADSRVVLDMP 702
Cdd:TIGR03925 228 LTAsrwseIRPALrDLIGTRIEL----RLGDPMDSEIDRRAAARVP 269
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
599-727 |
1.32e-03 |
|
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: 41.90 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2724155046 599 DFNKAVRSGKVKPLPgsertlttypyLLVIVDELADLMMVAPRDVDESIQRITQLARAAGIHLVLATQRPSvDIITgTIK 678
Cdd:COG0433 245 EARPEVGDADDRKLP-----------LVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDE-DVL 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2724155046 679 ANVPSRLAFATSSLADSRVV-----LDMPGAEKLI---GQGDALFLPMGESKPMRVQ 727
Cdd:COG0433 312 SQLGTQIILRLFNPRDQKAVkaaaeTLSEDLLERLpslGTGEALVLGEGIPLPVLVK 368
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
487-547 |
1.53e-03 |
|
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: 41.90 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2724155046 487 AIGIGKDVEGGY-VMANLAKM--PHMLVAGATGAGKSSFVNSMITSILMRatpdEVRMVLVDPK 547
Cdd:COG0433 25 GILIGKLLSPGVpVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFDPH 84
|
|
| |
