|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
351-837 |
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: 745.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 351 PSTELLRDYEQGSSEIDMQEIELNKQRIIDTLASFKMRVTPMKATVGPTVTLYEVVPDSGIKVSRIKTMEDDIAMSLKSE 430
Cdd:COG1674 138 PPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 431 GVRIIAPMPGQGTIGIEVPNSLPQTVSMRSILASRKFkeQQEKMELPIGIGKTITNEPFIFDLTKMPHLLIAGATGQGKS 510
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEF--QNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 511 VGLNALITSLLYSKRPEELKFVMVDPKMLEFSIYEEIekhflaklPDSDKAIITDMSRVVATLNSLCIEMDNRYHLLQHA 590
Cdd:COG1674 296 VCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGI--------PHLLTPVVTDPKKAANALKWAVREMERRYKLFAKA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 591 GraVRNIKEYNEQVRSGELRRID--GHEILPYIVLIVDEFADLMMTVGKEVEQPIARLAQKARAAGIHMVIATQRPSTDV 668
Cdd:COG1674 368 G--VRNIAGYNEKVREAKAKGEEeeGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 669 ITGLIKANFPARIAFKVFSMVDSRTVLDSPGANQLIGRGDMLFYQ--GKEMVRVQCAFMDTPETEAIVSHIAHQEStgsa 746
Cdd:COG1674 446 ITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPpgASKPIRVQGAFVSDEEVERVVDFLKSQGE---- 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 747 lilPEY---VPEGEDGGAKTFNPNEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGPQEGSKP 823
Cdd:COG1674 522 ---PEYieeILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKP 598
|
490
....*....|....
gi 918073585 824 REVFIKDQiSLEEL 837
Cdd:COG1674 599 REVLVSPE-ELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
297-827 |
1.07e-132 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 428.73 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 297 QPT-PQTRYSYPEHG----DEGDELQMIVEQAPEDDLVE-------DNHFSPEPTNPGVLLALYQKPSTELlrdyeqgsS 364
Cdd:PRK10263 809 QPVaPQPQYQQPQQPvapqPQYQQPQQPVAPQPQDTLLHpllmrngDSRPLHKPTTPLPSLDLLTPPPSEV--------E 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 365 EIDMQEIElNKQRIIDT-LASFKMRVTPMKATVGPTVTLYEVVPDSGIKVSRIKTMEDDIAMSLKSEGVRIIAPMPGQGT 443
Cdd:PRK10263 881 PVDTFALE-QMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPY 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 444 IGIEVPNSLPQTVSMRSILASRKFKEQQEKmeLPIGIGKTITNEPFIFDLTKMPHLLIAGATGQGKSVGLNALITSLLYS 523
Cdd:PRK10263 960 VGLELPNKKRQTVYLREVLDNAKFRDNPSP--LTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYK 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 524 KRPEELKFVMVDPKMLEFSIYEEIeKHFLAKlpdsdkaIITDMSRVVATLNSLCIEMDNRYHLLQHAGraVRNIKEYNEQ 603
Cdd:PRK10263 1038 AQPEDVRFIMIDPKMLELSVYEGI-PHLLTE-------VVTDMKDAANALRWCVNEMERRYKLMSALG--VRNLAGYNEK 1107
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 604 V-RSGELRR------------IDGH----EILPYIVLIVDEFADLMMTVGKEVEQPIARLAQKARAAGIHMVIATQRPST 666
Cdd:PRK10263 1108 IaEADRMMRpipdpywkpgdsMDAQhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSV 1187
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 667 DVITGLIKANFPARIAFKVFSMVDSRTVLDSPGANQLIGRGDMLfYQGKEM---VRVQCAFMDTPETEAIVShiaHQEST 743
Cdd:PRK10263 1188 DVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDML-YSGPNStlpVRVHGAFVRDQEVHAVVQ---DWKAR 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 744 GSalilPEYV------PEGEDGGAKTFNPNEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGP 817
Cdd:PRK10263 1264 GR----PQYVdgitsdSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSE 1339
|
570
....*....|
gi 918073585 818 QEGSKPREVF 827
Cdd:PRK10263 1340 QGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
458-665 |
1.09e-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: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 458 MRSILASRKFkeQQEKMELPIGIGKTITNEPFIFDLTKMP-HLLIAGATGQGKSVGLNALITSLLYSKRPEELKFVMVDP 536
Cdd:pfam01580 1 LLEVLESKPF--DTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 537 KMLEFSIYEEIeKHFLAklpdsdKAIITDMSRVVATLNSLCIEMDNRYHLLQHAGraVRNIKEYNEQVRSGELRR----- 611
Cdd:pfam01580 79 KMGELSAYEDI-PHLLS------VPVATDPKRALRALEWLVDEMERRYALFRALG--VRSIAGYNGEIAEDPLDGfgdvf 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 612 --IDGH----------EILPYIVLIVDEFADLMMTVGKE----VEQPIARLAQKARAAGIHMVIATQRPS 665
Cdd:pfam01580 150 lvIYGVhvmctagrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
767-829 |
7.56e-28 |
|
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: 106.73 E-value: 7.56e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918073585 767 NEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGPQEGSKPREVFIK 829
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
472-728 |
6.20e-25 |
|
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: 110.83 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 472 EKMELPIGIGKTitNEPFIFDLTK-----M-PHLLIAGATGQGKSVGLNALITSLLYSKRPEELKFVMVDPKMlefsiye 545
Cdd:TIGR03924 407 DRLRVPIGVGDD--GEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG------- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 546 eiEKHFL--AKLPDSdKAIITDM-------SRVVATLNSlciEMDNRYHLLQHAGrAVRNIKEYNEQVRSGelrriDGHE 616
Cdd:TIGR03924 478 --GATFLglEGLPHV-SAVITNLadeaplvDRMQDALAG---EMNRRQELLRAAG-NFANVAEYEKARAAG-----ADLP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 617 ILPYIVLIVDEF----------ADLMMTVGkeveqpiarlaQKARAAGIHMVIATQRPSTDVITGLiKANFPARIAFKVF 686
Cdd:TIGR03924 546 PLPALFVVVDEFsellsqhpdfADLFVAIG-----------RLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTF 613
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 918073585 687 SMVDSRTVLDSPGANQL---IGRGdMLFYQGKEMVRVQCAFMDTP 728
Cdd:TIGR03924 614 SASESRAVLGVPDAYHLpstPGAG-YLKVDTAEPVRFRAAYVSGP 657
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
60-221 |
2.46e-11 |
|
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: 62.99 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 60 LCLLAFMTVALFSVLTFLLSKGSDQSLiaplaegevleESSRSTA----NLFGIPGARLADYLFNrLLGWGIFFLFAYAL 135
Cdd:pfam13491 7 LLGLALLLLGLFLLLALVSYSPADPSW-----------STSGSGAapvhNWGGRFGAWLADLLLQ-LFGYSAWLLPVALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 136 YFIYHLIWRPGERilRYISRFllLGFLSLwtAIAMSALQHAFPSDTFLVW----GGTQGVRLYRYIQDSVGSAGLVVILG 211
Cdd:pfam13491 75 YWGWRLFRRRSLE--RRWLRL--LGFLLL--LLASSALFALRLPSLEFGLpggaGGVIGRLLANALVTLLGFTGATLLLL 148
|
170
....*....|
gi 918073585 212 FSLLIFAVLC 221
Cdd:pfam13491 149 ALLAIGLSLV 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
351-837 |
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: 745.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 351 PSTELLRDYEQGSSEIDMQEIELNKQRIIDTLASFKMRVTPMKATVGPTVTLYEVVPDSGIKVSRIKTMEDDIAMSLKSE 430
Cdd:COG1674 138 PPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 431 GVRIIAPMPGQGTIGIEVPNSLPQTVSMRSILASRKFkeQQEKMELPIGIGKTITNEPFIFDLTKMPHLLIAGATGQGKS 510
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEF--QNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 511 VGLNALITSLLYSKRPEELKFVMVDPKMLEFSIYEEIekhflaklPDSDKAIITDMSRVVATLNSLCIEMDNRYHLLQHA 590
Cdd:COG1674 296 VCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGI--------PHLLTPVVTDPKKAANALKWAVREMERRYKLFAKA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 591 GraVRNIKEYNEQVRSGELRRID--GHEILPYIVLIVDEFADLMMTVGKEVEQPIARLAQKARAAGIHMVIATQRPSTDV 668
Cdd:COG1674 368 G--VRNIAGYNEKVREAKAKGEEeeGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 669 ITGLIKANFPARIAFKVFSMVDSRTVLDSPGANQLIGRGDMLFYQ--GKEMVRVQCAFMDTPETEAIVSHIAHQEStgsa 746
Cdd:COG1674 446 ITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPpgASKPIRVQGAFVSDEEVERVVDFLKSQGE---- 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 747 lilPEY---VPEGEDGGAKTFNPNEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGPQEGSKP 823
Cdd:COG1674 522 ---PEYieeILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKP 598
|
490
....*....|....
gi 918073585 824 REVFIKDQiSLEEL 837
Cdd:COG1674 599 REVLVSPE-ELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
297-827 |
1.07e-132 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 428.73 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 297 QPT-PQTRYSYPEHG----DEGDELQMIVEQAPEDDLVE-------DNHFSPEPTNPGVLLALYQKPSTELlrdyeqgsS 364
Cdd:PRK10263 809 QPVaPQPQYQQPQQPvapqPQYQQPQQPVAPQPQDTLLHpllmrngDSRPLHKPTTPLPSLDLLTPPPSEV--------E 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 365 EIDMQEIElNKQRIIDT-LASFKMRVTPMKATVGPTVTLYEVVPDSGIKVSRIKTMEDDIAMSLKSEGVRIIAPMPGQGT 443
Cdd:PRK10263 881 PVDTFALE-QMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPY 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 444 IGIEVPNSLPQTVSMRSILASRKFKEQQEKmeLPIGIGKTITNEPFIFDLTKMPHLLIAGATGQGKSVGLNALITSLLYS 523
Cdd:PRK10263 960 VGLELPNKKRQTVYLREVLDNAKFRDNPSP--LTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYK 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 524 KRPEELKFVMVDPKMLEFSIYEEIeKHFLAKlpdsdkaIITDMSRVVATLNSLCIEMDNRYHLLQHAGraVRNIKEYNEQ 603
Cdd:PRK10263 1038 AQPEDVRFIMIDPKMLELSVYEGI-PHLLTE-------VVTDMKDAANALRWCVNEMERRYKLMSALG--VRNLAGYNEK 1107
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 604 V-RSGELRR------------IDGH----EILPYIVLIVDEFADLMMTVGKEVEQPIARLAQKARAAGIHMVIATQRPST 666
Cdd:PRK10263 1108 IaEADRMMRpipdpywkpgdsMDAQhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSV 1187
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 667 DVITGLIKANFPARIAFKVFSMVDSRTVLDSPGANQLIGRGDMLfYQGKEM---VRVQCAFMDTPETEAIVShiaHQEST 743
Cdd:PRK10263 1188 DVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDML-YSGPNStlpVRVHGAFVRDQEVHAVVQ---DWKAR 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 744 GSalilPEYV------PEGEDGGAKTFNPNEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGP 817
Cdd:PRK10263 1264 GR----PQYVdgitsdSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSE 1339
|
570
....*....|
gi 918073585 818 QEGSKPREVF 827
Cdd:PRK10263 1340 QGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
458-665 |
1.09e-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: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 458 MRSILASRKFkeQQEKMELPIGIGKTITNEPFIFDLTKMP-HLLIAGATGQGKSVGLNALITSLLYSKRPEELKFVMVDP 536
Cdd:pfam01580 1 LLEVLESKPF--DTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 537 KMLEFSIYEEIeKHFLAklpdsdKAIITDMSRVVATLNSLCIEMDNRYHLLQHAGraVRNIKEYNEQVRSGELRR----- 611
Cdd:pfam01580 79 KMGELSAYEDI-PHLLS------VPVATDPKRALRALEWLVDEMERRYALFRALG--VRSIAGYNGEIAEDPLDGfgdvf 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 612 --IDGH----------EILPYIVLIVDEFADLMMTVGKE----VEQPIARLAQKARAAGIHMVIATQRPS 665
Cdd:pfam01580 150 lvIYGVhvmctagrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
351-450 |
8.05e-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: 139.21 E-value: 8.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 351 PSTELLRDYEQGSSEIDMQEIELNKQRIIDTLASFKMRVTPMKATVGPTVTLYEVVPDSGIKVSRIKTMEDDIAMSLKSE 430
Cdd:pfam17854 2 PPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAP 81
|
90 100
....*....|....*....|
gi 918073585 431 GVRIIAPMPGQGTIGIEVPN 450
Cdd:pfam17854 82 SIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
767-829 |
1.92e-30 |
|
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: 114.00 E-value: 1.92e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918073585 767 NEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGPQEGSKPREVFIK 829
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
767-829 |
7.56e-28 |
|
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: 106.73 E-value: 7.56e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918073585 767 NEKDSLFDEVARMVVQTQVGSTSNIQRKFNIGYNRAGRLMDQLEGAGIVGPQEGSKPREVFIK 829
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
472-728 |
6.20e-25 |
|
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: 110.83 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 472 EKMELPIGIGKTitNEPFIFDLTK-----M-PHLLIAGATGQGKSVGLNALITSLLYSKRPEELKFVMVDPKMlefsiye 545
Cdd:TIGR03924 407 DRLRVPIGVGDD--GEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG------- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 546 eiEKHFL--AKLPDSdKAIITDM-------SRVVATLNSlciEMDNRYHLLQHAGrAVRNIKEYNEQVRSGelrriDGHE 616
Cdd:TIGR03924 478 --GATFLglEGLPHV-SAVITNLadeaplvDRMQDALAG---EMNRRQELLRAAG-NFANVAEYEKARAAG-----ADLP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 617 ILPYIVLIVDEF----------ADLMMTVGkeveqpiarlaQKARAAGIHMVIATQRPSTDVITGLiKANFPARIAFKVF 686
Cdd:TIGR03924 546 PLPALFVVVDEFsellsqhpdfADLFVAIG-----------RLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTF 613
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 918073585 687 SMVDSRTVLDSPGANQL---IGRGdMLFYQGKEMVRVQCAFMDTP 728
Cdd:TIGR03924 614 SASESRAVLGVPDAYHLpstPGAG-YLKVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
450-707 |
1.06e-20 |
|
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: 98.14 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 450 NSLPQTVSMRSILASRKFKEQQ-----------EKMELPIGI-GKtitNEPFIFDL-TKM--PHLLIAGATGQGKSVGLN 514
Cdd:TIGR03928 411 NSIPESVTFLEMYGVKKVEELNiqerwaknetyKSLAVPIGLrGK---DDIVYLNLhEKAhgPHGLVAGTTGSGKSEILQ 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 515 ALITSLLYSKRPEELKFVMVDPK---MLEfsIYEEIeKHFLAKLPDSDKAIItdmSRVVATLNSlciEMDNRYHLLQHAG 591
Cdd:TIGR03928 488 TYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNL-PHLLGTITNLDGAQS---MRALASIKA---ELKKRQRLFGENN 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 592 raVRNIKEYNEQVRSGELRridghEILPYIVLIVDEFADLmmtvgkEVEQP--IARLAQKA---RAAGIHMVIATQRPSt 666
Cdd:TIGR03928 559 --VNHINQYQKLYKQGKAK-----EPMPHLFLISDEFAEL------KSEQPefMKELVSTArigRSLGVHLILATQKPS- 624
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 918073585 667 DVITGLIKANFPARIAFKVFSMVDSRTVLDSPGANQLI--GRG 707
Cdd:TIGR03928 625 GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITvpGRA 667
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
60-221 |
2.46e-11 |
|
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: 62.99 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 60 LCLLAFMTVALFSVLTFLLSKGSDQSLiaplaegevleESSRSTA----NLFGIPGARLADYLFNrLLGWGIFFLFAYAL 135
Cdd:pfam13491 7 LLGLALLLLGLFLLLALVSYSPADPSW-----------STSGSGAapvhNWGGRFGAWLADLLLQ-LFGYSAWLLPVALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 136 YFIYHLIWRPGERilRYISRFllLGFLSLwtAIAMSALQHAFPSDTFLVW----GGTQGVRLYRYIQDSVGSAGLVVILG 211
Cdd:pfam13491 75 YWGWRLFRRRSLE--RRWLRL--LGFLLL--LLASSALFALRLPSLEFGLpggaGGVIGRLLANALVTLLGFTGATLLLL 148
|
170
....*....|
gi 918073585 212 FSLLIFAVLC 221
Cdd:pfam13491 149 ALLAIGLSLV 158
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
487-707 |
2.55e-10 |
|
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: 64.62 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 487 EPFIFDLTKMPHLLIAGATGQGKSVGLNALITSLLYSKRPEELKFVMVDpkmlefsiyeeiekhF-------LAKLPDSD 559
Cdd:TIGR03928 801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFD---------------FgtngllpLKKLPHVA 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 560 KAIITD----MSRVVATLNSlciEMDNRYHLLQHAGraVRNIKEYNEqvRSGELrridgheiLPYIVLIVDEFADLMMTV 635
Cdd:TIGR03928 866 DYFTLDeeekIEKLIRRIKK---EIDRRKKLFSEYG--VASISMYNK--ASGEK--------LPQIVIIIDNYDAVKEEP 930
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918073585 636 GKEVEQP-IARLAQKARAAGIHMVIATQRpSTDVITGLiKANFPARIAFKVFSMVDSRTVLDSPGANQ--LIGRG 707
Cdd:TIGR03928 931 FYEDFEElLIQLAREGASLGIYLVMTAGR-QNAVRMPL-MNNIKTKIALYLIDKSEYRSIVGRTKFTIeeIPGRG 1003
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
420-675 |
5.12e-10 |
|
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: 63.47 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 420 EDDIAMS--LKSEGVRIIAPMPGQGTIGIEVpnsLPQTVSMRSILASRKFKEQQEKMELPIGIgKTITNEPFIFDLTKMP 497
Cdd:TIGR03928 1022 EDDLEVIenIKAEIQKMNEAWTGERPKPIPM---VPEELSLEEFRERYEVRKILEEGSIPIGL-DEETVEPVYIDLTENP 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 498 HLLIAGATGQGKSVGLNALITSLLYSkrpEELKFVMVDpkmlefSIYEEIEKHflAKLPDSdKAIITDMSRVVATLNSLC 577
Cdd:TIGR03928 1098 HLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLID------SIDRGLLAY--RDLKEV-ATYIEEKEDLKEILAELK 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 578 IEMDNRYHLLQHAGRAVRNIKEYNEqvrsgelrridgheilpyIVLIVDEFADLMMTVGKEVEQPIARLAQKARAAGIHM 657
Cdd:TIGR03928 1166 EEIELREAAYKEALQNETGEPAFKP------------------ILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHF 1227
|
250 260
....*....|....*....|..
gi 918073585 658 VIATQRP----STDVITGLIKA 675
Cdd:TIGR03928 1228 IVAGTHSelskSYDGVPKEIKQ 1249
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
452-660 |
1.47e-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: 55.00 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 452 LPQTVSMRSILAsrkfKEQQEKMELPIGIGKTiTNEPFIFDLTKMPHLLIAGATGQGKSVGLNALITSLLYSKRPEELKF 531
Cdd:TIGR03925 324 LPARLPLSALPA----GGGAPRLRVPLGLGES-DLAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 532 VMVDPKMlefSIYEEIEKHFLAklpdsdkAIITDMSRVVATLNSLCIEMDNRyhlLQHAGravrnikeyneqVRSGELRR 611
Cdd:TIGR03925 399 VVVDYRR---TLLGAVPEDYLA-------GYAATSAALTELIAALAALLERR---LPGPD------------VTPQQLRA 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 918073585 612 ID---GHEilpyIVLIVDEFaDLMMTVGKEVEQPIARLAQKARAAGIHMVIA 660
Cdd:TIGR03925 454 RSwwsGPE----IYVVVDDY-DLVATGSGNPLAPLVELLPHARDIGLHVVVA 500
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
452-754 |
2.61e-06 |
|
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: 51.15 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 452 LPQTVSMRSILAS------RKFKEQQEKMELPIGIgktiTNEPF-------IFDLTKMP-HLLIAGATGQGKSVGLNALI 517
Cdd:TIGR03925 25 LPEPPALDDLLPRldvdpwRVDYGQRGRLTVPVGI----VDRPFeqrqdplVVDLSGAAgHVAIVGAPQSGKSTALRTLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 518 TSLLYSKRPEELKFVMVD---PKMLEfsiyeeiekhfLAKLP---------DSDKAiitdmSRVVATLNSLcieMDNRYH 585
Cdd:TIGR03925 101 LALALTHTPEEVQFYCLDfggGGLAS-----------LADLPhvggvagrlDPERV-----RRTVAEVEGL---LRRRER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 586 LLqhAGRAVRNIKEYNEQVRSGELRRidgheiLPY--IVLIVD-------EFADLmmtvgkevEQPIARLAQKARAAGIH 656
Cdd:TIGR03925 162 LF--RTHGIDSMAQYRARRAAGRLPE------DPFgdVFLVIDgwgtlrqDFEDL--------EDKVTDLAARGLAYGVH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 657 MVIATQRpSTDVITGLiKANFPARIAFK----VFSMVDSRTVLDSPgaNQLIGRGdmLFYQGKEMV----RVQ-CAFMDT 727
Cdd:TIGR03925 226 VVLTASR-WSEIRPAL-RDLIGTRIELRlgdpMDSEIDRRAAARVP--AGRPGRG--LTPDGLHMLialpRLDgIASVDD 299
|
330 340 350
....*....|....*....|....*....|
gi 918073585 728 PETEAIVSHIA---HQESTGSALILPEYVP 754
Cdd:TIGR03925 300 LGTRGLVAVIRdvwGGPPAPPVRLLPARLP 329
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
480-536 |
1.03e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 45.71 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 480 IGKTITNEPFIFDL---TKMPHLLIAGATGQGKSVGLNALITSLLYSKRpeelKFVMVDP 536
Cdd:COG3451 185 LLNTRSGTPVFFDFhdgLDNGNTLILGPSGSGKSFLLKLLLLQLLRYGA----RIVIFDP 240
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
477-665 |
2.47e-04 |
|
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: 44.21 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 477 PIGIGKTI-TNEPFIFDLTKM--PHLLIAGATGQGKSVGLNALITSLL--------------YSK--------------R 525
Cdd:COG0433 25 GILIGKLLsPGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSragvpvlvfdphgeYSGlaepgaeradvgvfD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 526 PEELKFVMVDPKMLEFSIyEEIEKHFLAKLPDSD--------------------------KAIITDMSRVVATLNS---- 575
Cdd:COG0433 105 PGAGRPLPINPWDLFATA-SELGPLLLSRLDLNDtqrgvlrealrladdkglllldlkdlIALLEEGEELGEEYGNvsaa 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918073585 576 ------------------LCIEMDNRYHLLQHAGRAVR-NIKEYNEQVRS-------GEL-----RRIDGHEILPYIVLI 624
Cdd:COG0433 184 sagallrrleslesadglFGEPGLDLEDLLRTDGRVTViDLSGLPEELQStfvlwllRELfearpEVGDADDRKLPLVLV 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 918073585 625 VDEFADLMMTVGKEVEQPIARLAQKARAAGIHMVIATQRPS 665
Cdd:COG0433 264 IDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS 304
|
|
| |
