|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
1-334 |
1.63e-161 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 454.03 E-value: 1.63e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 1 MKKIALIVVILAAAVAGAWWFdlpvrlgFAGETRQA-VLYGNVDIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDD 79
Cdd:PRK03598 4 KVVIGLAVVVLAAAVAGGWWW-------YQSRQDNGlTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 80 EPFRQTLDASEAEAEASRATLTKLKAGARAGEIAQARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAA 159
Cdd:PRK03598 77 APYENALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 160 AAARARSAREGLALLEEGSRVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLSL 239
Cdd:PRK03598 157 AQATLKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 240 TEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPKSVETPELRTDLVYRLRIVITNPGKDLRQ 319
Cdd:PRK03598 237 TRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQ 316
|
330
....*....|....*
gi 501008715 320 GMPVTVQLPETKEAS 334
Cdd:PRK03598 317 GMPVTVRFADEAGHE 331
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-327 |
4.77e-69 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 218.76 E-value: 4.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 1 MKKIALIVVILAAAVAGAWWFdlpvrlGFAGETRQAVLYGNVDIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDE 80
Cdd:COG1566 6 KRRLLALVLLLLALGLALWAA------GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 81 PFRQTLDASEAEAEASRATLTKLKAGARAG-EIAQARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAA 159
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEaEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 160 AAARARSAREGLALLEEGSRV-EDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLS 238
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 239 LTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPkSVETPELRTDLVYRLRIVITNP-GKDL 317
Cdd:COG1566 240 PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS-PPKNATGNVVQRYPVRIRLDNPdPEPL 318
|
330
....*....|
gi 501008715 318 RQGMPVTVQL 327
Cdd:COG1566 319 RPGMSATVEI 328
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
22-328 |
1.59e-32 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 123.19 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 22 DLPVRLGFAGETRQavlygnvdIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRATLt 101
Cdd:TIGR01730 10 TLANTLTFPGSLEA--------VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 102 klkagarageiaqaratheerlaelENAELAYERAKQLRPNGTISQAELDQSSAGRAAAAARARSAREGLALLEEgsrve 181
Cdd:TIGR01730 81 -------------------------ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQL----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 182 ditsaeaqvdaaaakaasartSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGM 261
Cdd:TIGR01730 131 ---------------------NLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQ 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501008715 262 KVTIASDTAPGRAYEGTVGFISPVAEftpksvetpelRTDLVYRLRIVITNPGKDLRQGMPVTVQLP 328
Cdd:TIGR01730 190 TLTVELDALPGEEFKGKLRFIDPRVD-----------SGTGTVRVRATFPNPDGRLLPGMFGRVTIS 245
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
45-308 |
1.54e-19 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 87.48 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 45 RQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAE---AEASRATLTKLKAGARAGEIA-------- 113
Cdd:pfam00529 19 NAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQlakAQAQVARLQAELDRLQALESElaisrqdy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 114 --------QARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAAAAARARSAREGLALLEEGS------- 178
Cdd:pfam00529 99 dgataqlrAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQItqsaaen 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 179 ---RVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSR-VRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDL 254
Cdd:pfam00529 179 qaeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLsVTVDGGTVSAGLRLMFVVPEDNLLVPGMFVETQL 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501008715 255 GRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPKSVETPELRTDLVYRLRI 308
Cdd:pfam00529 259 DQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
1-334 |
1.63e-161 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 454.03 E-value: 1.63e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 1 MKKIALIVVILAAAVAGAWWFdlpvrlgFAGETRQA-VLYGNVDIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDD 79
Cdd:PRK03598 4 KVVIGLAVVVLAAAVAGGWWW-------YQSRQDNGlTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 80 EPFRQTLDASEAEAEASRATLTKLKAGARAGEIAQARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAA 159
Cdd:PRK03598 77 APYENALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 160 AAARARSAREGLALLEEGSRVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLSL 239
Cdd:PRK03598 157 AQATLKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 240 TEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPKSVETPELRTDLVYRLRIVITNPGKDLRQ 319
Cdd:PRK03598 237 TRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQ 316
|
330
....*....|....*
gi 501008715 320 GMPVTVQLPETKEAS 334
Cdd:PRK03598 317 GMPVTVRFADEAGHE 331
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-327 |
4.77e-69 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 218.76 E-value: 4.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 1 MKKIALIVVILAAAVAGAWWFdlpvrlGFAGETRQAVLYGNVDIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDE 80
Cdd:COG1566 6 KRRLLALVLLLLALGLALWAA------GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 81 PFRQTLDASEAEAEASRATLTKLKAGARAG-EIAQARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAA 159
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEaEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 160 AAARARSAREGLALLEEGSRV-EDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLS 238
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 239 LTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPkSVETPELRTDLVYRLRIVITNP-GKDL 317
Cdd:COG1566 240 PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS-PPKNATGNVVQRYPVRIRLDNPdPEPL 318
|
330
....*....|
gi 501008715 318 RQGMPVTVQL 327
Cdd:COG1566 319 RPGMSATVEI 328
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
33-328 |
9.05e-46 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 158.18 E-value: 9.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 33 TRQAVLYGNVD-IRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRAtltklkagarage 111
Cdd:COG0845 9 PETVEATGTVEaRREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQA------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 112 iaqaratheerlaELENAELAYERAKQLRPNGTISQAELDQSSAGRAAAAARARSAREGLALLeegsrveditsaeaqvd 191
Cdd:COG0845 76 -------------QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQA----------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 192 aaaakaasaRTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAP 271
Cdd:COG0845 126 ---------RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGP 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 501008715 272 GRAYEGTVGFISPVAEftpksvetPELRTdlvYRLRIVITNPGKDLRQGMPVTVQLP 328
Cdd:COG0845 197 GKTFEGKVTFIDPAVD--------PATRT---VRVRAELPNPDGLLRPGMFVRVRIV 242
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
22-328 |
1.59e-32 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 123.19 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 22 DLPVRLGFAGETRQavlygnvdIRQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRATLt 101
Cdd:TIGR01730 10 TLANTLTFPGSLEA--------VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 102 klkagarageiaqaratheerlaelENAELAYERAKQLRPNGTISQAELDQSSAGRAAAAARARSAREGLALLEEgsrve 181
Cdd:TIGR01730 81 -------------------------ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQL----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 182 ditsaeaqvdaaaakaasartSLKDTELVAPNDGVVLSRVRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGM 261
Cdd:TIGR01730 131 ---------------------NLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQ 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501008715 262 KVTIASDTAPGRAYEGTVGFISPVAEftpksvetpelRTDLVYRLRIVITNPGKDLRQGMPVTVQLP 328
Cdd:TIGR01730 190 TLTVELDALPGEEFKGKLRFIDPRVD-----------SGTGTVRVRATFPNPDGRLLPGMFGRVTIS 245
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
2-283 |
8.87e-20 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 88.55 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 2 KKIALIVVILA-AAVAGAWWfdlpvRLGFAGETRQAVLYGNVdIRQVSlgfRVSGRIAELRVDEGDSVRKGDVIARLDDE 80
Cdd:PRK10476 12 KLPALAIVALAiVALVFVIW-----RTDSAPSTDDAYIDADV-VHVAS---EVGGRIVELAVTENQAVKKGDLLFRIDPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 81 PFRQTLDASEAEAEASRATL--TKLKAGARAGEIAQARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRA 158
Cdd:PRK10476 83 PYELTVAQAQADLALADAQImtTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 159 AAAARARSareglALLEE---GSRVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPADVVY 235
Cdd:PRK10476 163 DAEVSLNQ-----ALLQAqaaAAAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501008715 236 VLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFIS 283
Cdd:PRK10476 238 TLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIG 285
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
45-308 |
1.54e-19 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 87.48 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 45 RQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAE---AEASRATLTKLKAGARAGEIA-------- 113
Cdd:pfam00529 19 NAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQlakAQAQVARLQAELDRLQALESElaisrqdy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 114 --------QARATHEERLAELENAELAYERAKQLRPNGTISQAELDQSSAGRAAAAARARSAREGLALLEEGS------- 178
Cdd:pfam00529 99 dgataqlrAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQItqsaaen 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 179 ---RVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSR-VRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDL 254
Cdd:pfam00529 179 qaeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLsVTVDGGTVSAGLRLMFVVPEDNLLVPGMFVETQL 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501008715 255 GRLYPGMKVTIASDTAPGRAYEGTVGFISPVAEFTPKSVETPELRTDLVYRLRI 308
Cdd:pfam00529 259 DQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
33-321 |
1.09e-16 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 77.55 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 33 TRQAVLYGNVDI---RQVSLGFRVSGRIAELRVD-EGDSVRKGDVIARLDDEpfrqtlDASEAEAEasratLTKLKAGAR 108
Cdd:pfam16576 3 SRTIRAVGRVAYderRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSP------ELVAAQQE-----YLLALRSGD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 109 AGEIAQARATHEERLAELEnaelayerakqlrpngtISQAELDQssagraaaaararsareglalLEEGsrveditsaea 188
Cdd:pfam16576 72 ALSKSELLRAARQRLRLLG-----------------MPEAQIAE---------------------LERT----------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 189 qvdaaaakaasaRTSLKDTELVAPNDGVVLSR-VREtGAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIAS 267
Cdd:pfam16576 103 ------------GKVQPTVTVYAPISGVVTELnVRE-GMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTL 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501008715 268 DTAPGRAYEGTVGFISPVAEftpksvetPELRTdlvYRLRIVITNPGKDLRQGM 321
Cdd:pfam16576 170 PALPGKTFEGKVDYIYPTLD--------PKTRT---VRVRIELPNPDGRLKPGM 212
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
4-333 |
1.16e-15 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 76.74 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 4 IALIVVILAAAVAGAWWFDLPVR-----LGFAGETRQAVL-YGNVD-IRQVSLGFRVSGRIAELRVDEGDSVRKGDVIAR 76
Cdd:PRK11578 12 LIALVIVLAGGITLWRILNAPVPtyqtlIVRPGDLQQSVLaTGKLDaLRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 77 LDDEPfrqtldaSEAEAEASRATLTKLKAgaragEIAQARatheerlAELENAELAYERAKQLRPNGTISQAELDQssag 156
Cdd:PRK11578 92 IDPEQ-------AENQIKEVEATLMELRA-----QRQQAE-------AELKLARVTLSRQQRLAKTQAVSQQDLDT---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 157 raaaaararsareglALLEEGSRVEDITSAEAQVDAAAAKAASARTSLKDTELVAPNDGVVLSRVRETGAIVSPA-DVVY 235
Cdd:PRK11578 149 ---------------AATELAVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAqQAPN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 236 VLSLTE--PVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPvaeftpksveTPELRTDLV-YRLRIVITN 312
Cdd:PRK11578 214 ILTLADmsTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILP----------TPEKVNDAIfYYARFEVPN 283
|
330 340
....*....|....*....|...
gi 501008715 313 PGKDLRQGMP--VTVQLPETKEA 333
Cdd:PRK11578 284 PNGLLRLDMTaqVHIQLTDVKNV 306
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
208-317 |
7.63e-13 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 63.92 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 208 ELVAPNDGVVLSRVRETGAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVAE 287
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100 110
....*....|....*....|....*....|
gi 501008715 288 ftpksvetpelRTDLVYRLRIVITNPGKDL 317
Cdd:pfam13437 81 -----------PDTGVIPVRVSIENPKTPI 99
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
55-328 |
1.30e-11 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 65.03 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 55 GRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRATLTKLKA-------------------GARAGEIAQA 115
Cdd:TIGR01843 52 GIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAeadsqaaiefpddllsaedPAVPELIKGQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 116 RATHEERLAELEN-----------------------------AELAYERAKQLRP---NGTIS--------------QAE 149
Cdd:TIGR01843 132 QSLFESRKSTLRAqlelilaqikqleaelaglqaqlqalrqqLEVISEELEARRKlkeKGLVSrlellelereraeaQGE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 150 LDQSSAGRAAAAARARSAREGLALLEEgSRVEDITSAEAQVDAAAAKAASARTSLKD----TELVAPNDGVVLS-RVRET 224
Cdd:TIGR01843 212 LGRLEAELEVLKRQIDELQLERQQIEQ-TFREEVLEELTEAQARLAELRERLNKARDrlqrLIIRSPVDGTVQSlKVHTV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 225 GAIVSPA-DVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAY---EGTVGFISpvaeftPKSVETPELRt 300
Cdd:TIGR01843 291 GGVVQPGeTLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYgilNGKVKSIS------PDTFTDERGG- 363
|
330 340 350
....*....|....*....|....*....|....*
gi 501008715 301 DLVYRLRIVITNP-------GKDLRQGMPVTVQLP 328
Cdd:TIGR01843 364 GPYYRVRISIDQNtlgigpkGLELSPGMPVTADIK 398
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
45-91 |
2.43e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 46.67 E-value: 2.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 501008715 45 RQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEA 91
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
2-268 |
5.42e-06 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 47.77 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 2 KKIALI----VVILAAAVAGAWWFdlpVRLGFAGETRQAVLYGNvdirQVSLGFRVSGRIAELRVDEGDSVRKGDVIARL 77
Cdd:PRK15136 20 RKRALLlltlLFIIIGVAYGIYWF---LVLRHHQETDDAYVAGN----QVQIMSQVSGSVTKVWADNTDFVKEGDVLVTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 78 DDEPFRQTLD-ASEAEAEASRAT------LTKLKAG--ARAGEIAQARATHEERLAeLENAEL-AYERAKQLRPNGTISQ 147
Cdd:PRK15136 93 DPTDAEQAFEkAKTALANSVRQThqlminSKQYQANieLQKTALAQAQSDLNRRVP-LGNANLiGREELQHARDAVASAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 148 AELDqssagraaAAARARSAREGLAL---LEEGSRVEDITSAEAQVDAaaakaasartSLKDTELVAPNDGVVLSRVRET 224
Cdd:PRK15136 172 AQLD--------VAIQQYNANQAMILntpLEDQPAVQQAATEVRNAWL----------ALQRTKIVSPMTGYVSRRSVQV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 501008715 225 GAIVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASD 268
Cdd:PRK15136 234 GAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSD 277
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
4-151 |
1.22e-04 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 43.63 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 4 IALIVVILAAAVAGAWWFDL-------------------------------PVRLGFAgeTRQAVLY-----GNVD-IRQ 46
Cdd:PRK11556 10 VIVIVVVIAAIAAFWFWQGRstsssaapgaakqaqqspaggrrgmrsgplaPVQAATA--TEQAVPRyltglGTVTaANT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 47 VSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLdaseAEAEasratltklkagaraGEIAQARATheerlaeL 126
Cdd:PRK11556 88 VTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVAL----AQAQ---------------GQLAKDQAT-------L 141
|
170 180
....*....|....*....|....*
gi 501008715 127 ENAELAYERAKQLRPNGTISQAELD 151
Cdd:PRK11556 142 ANARRDLARYQQLAKTNLVSRQELD 166
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-151 |
1.06e-03 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 40.55 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 45 RQVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASE---AEAEAS-RATLTKLKagaRAGEIAQARATHE 120
Cdd:PRK09578 62 RQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAgalAKAEAAhLAALDKRR---RYDDLVRDRAVSE 138
|
90 100 110
....*....|....*....|....*....|.
gi 501008715 121 ERLAELENAELAyERAKQLRPNGTISQAELD 151
Cdd:PRK09578 139 RDYTEAVADERQ-AKAAVASAKAELARAQLQ 168
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
4-135 |
3.77e-03 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 38.57 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 4 IALIVVILAA-AVAGAWWF--DLPVrlgfageTRQAVLYGNVdirqVSLGFRVSGRIAELRVDEGDSVRKGDVIARLDDE 80
Cdd:PRK10559 13 ITLVLVILAFiAIFRAWVFytESPW-------TRDARFSADV----VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501008715 81 PFRQTLDASEAE--------AEASRATLTKLKAGARA---GEIAQAR---ATHEERLA----ELENAELAYER 135
Cdd:PRK10559 82 RYQKALAEAEADvayyqvlaQEKRREAGRRNRLGVQAmsrEEIDQANnvlQTVLHQLAkaqaTRDLAKLDLER 154
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
52-329 |
3.96e-03 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 38.54 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 52 RVSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDA-----SEAEAEASRATLTKLKAGARAGEIAQARATHEERLAEL 126
Cdd:PRK09859 67 QVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSakgslAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 127 ENAElayerakqlrPNGTISQAELDQSSAGraaaaararsareglalLEEGSRVEDITSaeaqvdaaaakaASARTSLKD 206
Cdd:PRK09859 147 NEAE----------ANVTVAKAAVEQATIN-----------------LQYANVTSPITG------------VSGKSSVTV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 207 TELVAPNDGVVLSRVREtgaiVSPADVVYVLSLTEPVWVRAYVAEPDLGRLYPGMKVTIASDTAPGRAYEGTVGFISPVA 286
Cdd:PRK09859 188 GALVTANQADSLVTVQR----LDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTV 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 501008715 287 EFTPKSVEtpelrtdlvyrLRIVITNPGKDLRQGMPVTVQLPE 329
Cdd:PRK09859 264 DETTGSVT-----------LRAIFPNPNGDLLPGMYVTALVDE 295
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
53-121 |
7.19e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 37.88 E-value: 7.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501008715 53 VSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRATLTKLKAGARAGEIAQARATHEE 121
Cdd:PRK11855 168 VAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAA 236
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
53-132 |
7.28e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 37.89 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008715 53 VSGRIAELRVDEGDSVRKGDVIARLDDEPFRQTLDASEAEAEASRATLTKLKAGARAGEIAQARATHEERLAELENAELA 132
Cdd:PRK05704 52 AAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDAS 131
|
|
| |
