|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
38-369 |
3.59e-91 |
|
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: 276.44 E-value: 3.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 38 RPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANLEYAR 117
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 118 NNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSlqpVT 197
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG---TP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 198 LATIYKDDLLYTYFNITDNQwlAMLMQQGTaqqkdtlprQITVNLGEDGIQPYPATLDYFAPNVDLSTGTLNLRARLDNP 277
Cdd:COG0845 159 LFTIADLDPLEVEFDVPESD--LARLKVGQ---------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 278 KGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVNDSDRVRYRHIEVGQlIDDTLRQITGGLSPQERYVTRA 357
Cdd:COG0845 228 DGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGR-RDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|..
gi 189437920 358 LMKVREGMKVKP 369
Cdd:COG0845 307 LQRLRDGAKVRV 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-370 |
2.79e-67 |
|
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: 215.26 E-value: 2.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 34 ISVARPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANL 113
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 114 EYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSl 193
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 194 qpVTLATIYKDDLLYTYFNITDnqwlamlmqQGTAQQKDTLPRQITVNlGEDGIQpYPATLDYFAPNVDLSTGTLNLRAR 273
Cdd:TIGR01730 160 --QTLATIVDLDPLEADFSVPE---------RDLPQLRRGQTLTVELD-ALPGEE-FKGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 274 LDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVNDSDRVRYRHIEVGQLIDDtLRQITGGLSPQERY 353
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGG-YVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 189437920 354 VTRALMKVREGMKVKPT 370
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
15-368 |
2.59e-40 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 146.78 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 15 LAGCGDKrEAARGAMPVPEISVARPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTI 94
Cdd:PRK15030 22 LTGCDDK-QAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 95 YQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPF 174
Cdd:PRK15030 101 YQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 175 DGTVSRNQVDAGSYVGGSlQPVTLATIYKDDLLYTYFNITDNQWLAMLMQ--QGTAQQKDTLPRQITVNlgEDGIQ-PYP 251
Cdd:PRK15030 181 SGRIGKSNVTEGALVQNG-QATALATVQQLDPIYVDVTQSSNDFLRLKQElaNGTLKQENGKAKVSLIT--SDGIKfPQD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 252 ATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGK-YVYVVNDSDRVRYRHI 330
Cdd:PRK15030 258 GTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETRPI 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 189437920 331 EVGQLIDDTLrQITGGLSPQERYVTRALMKVREGMKVK 368
Cdd:PRK15030 338 VASQAIGDKW-LVTEGLKAGDRVVISGLQKVRPGVQVK 374
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-355 |
2.02e-28 |
|
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: 112.90 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 56 SEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQI 135
Cdd:pfam00529 17 SGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 136 QVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGtVSRNQ-VDAGSYVgGSLQPVTLATIYKDDLLYTYFNIT 214
Cdd:pfam00529 97 DYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGG-ISRESlVTAGALV-AQAQANLLATVAQLDQIYVQITQS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 215 DNQWLAMLMQQGTAQQKDTLPRQITVNLGEDGIQ------PYPATLDYFAPNVDLSTGTLNLRARLDNP-KGLLKSGLYV 287
Cdd:pfam00529 175 AAENQAEVRSELSGAQLQIAEAEAELKLAKLDLErteiraPVDGTVAFLSVTVDGGTVSAGLRLMFVVPeDNLLVPGMFV 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189437920 288 SITLPYGKESQAILIP-DASIGTDQLGKYVYVVNDSDRVRYRHIEVGQLIDDtLRQITGGLSPQERYVT 355
Cdd:pfam00529 255 ETQLDQVRVGQPVLIPfDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGP-YYPLRIGLSAGALVRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
38-369 |
3.59e-91 |
|
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: 276.44 E-value: 3.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 38 RPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANLEYAR 117
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 118 NNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSlqpVT 197
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG---TP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 198 LATIYKDDLLYTYFNITDNQwlAMLMQQGTaqqkdtlprQITVNLGEDGIQPYPATLDYFAPNVDLSTGTLNLRARLDNP 277
Cdd:COG0845 159 LFTIADLDPLEVEFDVPESD--LARLKVGQ---------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 278 KGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVNDSDRVRYRHIEVGQlIDDTLRQITGGLSPQERYVTRA 357
Cdd:COG0845 228 DGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGR-RDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|..
gi 189437920 358 LMKVREGMKVKP 369
Cdd:COG0845 307 LQRLRDGAKVRV 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-370 |
2.79e-67 |
|
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: 215.26 E-value: 2.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 34 ISVARPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANL 113
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 114 EYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSl 193
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 194 qpVTLATIYKDDLLYTYFNITDnqwlamlmqQGTAQQKDTLPRQITVNlGEDGIQpYPATLDYFAPNVDLSTGTLNLRAR 273
Cdd:TIGR01730 160 --QTLATIVDLDPLEADFSVPE---------RDLPQLRRGQTLTVELD-ALPGEE-FKGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 274 LDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVNDSDRVRYRHIEVGQLIDDtLRQITGGLSPQERY 353
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGG-YVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 189437920 354 VTRALMKVREGMKVKPT 370
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
15-368 |
2.59e-40 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 146.78 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 15 LAGCGDKrEAARGAMPVPEISVARPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTI 94
Cdd:PRK15030 22 LTGCDDK-QAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 95 YQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPF 174
Cdd:PRK15030 101 YQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 175 DGTVSRNQVDAGSYVGGSlQPVTLATIYKDDLLYTYFNITDNQWLAMLMQ--QGTAQQKDTLPRQITVNlgEDGIQ-PYP 251
Cdd:PRK15030 181 SGRIGKSNVTEGALVQNG-QATALATVQQLDPIYVDVTQSSNDFLRLKQElaNGTLKQENGKAKVSLIT--SDGIKfPQD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 252 ATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGK-YVYVVNDSDRVRYRHI 330
Cdd:PRK15030 258 GTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETRPI 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 189437920 331 EVGQLIDDTLrQITGGLSPQERYVTRALMKVREGMKVK 368
Cdd:PRK15030 338 VASQAIGDKW-LVTEGLKAGDRVVISGLQKVRPGVQVK 374
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
9-370 |
1.55e-36 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 136.46 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 9 LTLIPLLAGCGD-KREAARGAMPVPEISVARPVVkdITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVL 87
Cdd:PRK09578 14 LVALFVLAGCGKgDSDAAAAAPREATVVTVRPTS--VPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 88 FVIEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGY 167
Cdd:PRK09578 92 FRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 168 CTVRAPFDGTVSRNQVDAGSYVGGSlQPVTLATIYKDDLLYTYFN--ITDNQWLAMLMQQGTAQ---QKDtlprqITVNL 242
Cdd:PRK09578 172 ATVTAPIDGRARRALVTEGALVGQD-QATPLTTVEQLDPIYVNFSqpAADVEALRRAVKSGRATgiaQQD-----VAVTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 243 -GEDGIQ-PYPATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIP-DASIGTDQLGKyVYVV 319
Cdd:PRK09578 246 vRADGSEyPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPrDALLRTADSAS-VKVV 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 189437920 320 NDSDRVRYRHIEVGQLIDDTLRqITGGLSPQERYVTRALMKVREGMKVKPT 370
Cdd:PRK09578 325 GQNGKVRDVEVEADQMSGRDWI-VTRGLAGGERVIVDNAAQFAPGTAVKAV 374
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
16-367 |
2.51e-35 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 133.76 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 16 AGCGDKREAARGAMPVPeisvarpVVKDITLTKEYPGYLS------SEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFV 89
Cdd:PRK11556 45 QSPAGGRRGMRSGPLAP-------VQAATATEQAVPRYLTglgtvtAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 90 IEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNLGYCT 169
Cdd:PRK11556 118 IDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 170 VRAPFDGTVSRNQVDAGSYV--GGSLQPVTLATIYKDDLLYTyfnITDNQWLAMLMQQGTAQqkdTLP-----RQITVNL 242
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQIssGDTTGIVVITQTHPIDLVFT---LPESDIATVVQAQKAGK---PLVveawdRTNSKKL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 243 GEdgiqpypATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVNDS 322
Cdd:PRK11556 272 SE-------GTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDE 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 189437920 323 DRVRYRHIEVGqlIDDTLRQ-ITGGLSPQERYVTRALMKVREGMKV 367
Cdd:PRK11556 345 NKVSKHLVTPG--IQDSQKVvISAGLSAGDRVVTDGIDRLTEGAKV 388
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
11-371 |
2.81e-35 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 132.92 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 11 LIPLLAgCG------DKREAARGAMPVPEISVARPVVKDITLTKEYPGYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKG 84
Cdd:PRK09859 8 LIPLLF-CGamltacDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 85 QVLFVIEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTN 164
Cdd:PRK09859 87 DSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATIN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 165 LGYCTVRAPFDGTVSRNQVDAGSYVGGSlQPVTLATIYKDDLLYTYFNITDNQWLAML--MQQGTAQQ-KDTLPRQITVN 241
Cdd:PRK09859 167 LQYANVTSPITGVSGKSSVTVGALVTAN-QADSLVTVQRLDPIYVDLTQSVQDFLRMKeeVASGQIKQvQGSTPVQLNLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 242 LGEDGIQpyPATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGTDQLGKYVYVVND 321
Cdd:PRK09859 246 NGKRYSQ--TGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILD 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 189437920 322 SDR-VRYRHIEVGQLIDDTLrQITGGLSPQERYVTRALMKVREGMKVKPTS 371
Cdd:PRK09859 324 KDDvVQLREIEASKAIGDQW-VVTSGLQAGDRVIVSGLQRIRPGIKARAIS 373
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-355 |
2.02e-28 |
|
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: 112.90 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 56 SEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQI 135
Cdd:pfam00529 17 SGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 136 QVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGtVSRNQ-VDAGSYVgGSLQPVTLATIYKDDLLYTYFNIT 214
Cdd:pfam00529 97 DYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGG-ISRESlVTAGALV-AQAQANLLATVAQLDQIYVQITQS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 215 DNQWLAMLMQQGTAQQKDTLPRQITVNLGEDGIQ------PYPATLDYFAPNVDLSTGTLNLRARLDNP-KGLLKSGLYV 287
Cdd:pfam00529 175 AAENQAEVRSELSGAQLQIAEAEAELKLAKLDLErteiraPVDGTVAFLSVTVDGGTVSAGLRLMFVVPeDNLLVPGMFV 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189437920 288 SITLPYGKESQAILIP-DASIGTDQLGKYVYVVNDSDRVRYRHIEVGQLIDDtLRQITGGLSPQERYVT 355
Cdd:pfam00529 255 ETQLDQVRVGQPVLIPfDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGP-YYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
52-291 |
3.66e-26 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 107.06 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 52 GYLSSEkTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARA-------------------- 111
Cdd:COG1566 39 GRVEAR-VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAqlarleaelgaeaeiaaaea 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 112 -------NLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAA---------------------------VSNAEAA 157
Cdd:COG1566 118 qlaaaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeeelaaaqaqVAQAEAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 158 LNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSlQPvtLATIYKDDLLYTYFNITDNQwlAMLMQQGTaqqkdtlPRQ 237
Cdd:COG1566 198 LAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAG-QP--LLTIVPLDDLWVEAYVPETD--LGRVKPGQ-------PVE 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189437920 238 ITVNLGEDgiQPYPATLDYFAPNV------DLSTGTLNL----RARLDNPKGL-LKSGLYVSITL 291
Cdd:COG1566 266 VRVDAYPD--RVFEGKVTSISPGAgftsppKNATGNVVQrypvRIRLDNPDPEpLRPGMSATVEI 328
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
78-356 |
1.02e-25 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 104.44 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 78 GSRVRKGQVLFVIEPTIYQDnvkqTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAA 157
Cdd:TIGR00999 1 GDPVKKGQVLAVVDSPELAK----MAAELKVAQKRVELARKTYEREKKLFEQGVIPRQEFESAEYALEEAQAEVQAAKSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 158 LNTAR--TNLGYCTVRAPFDGTVSRNQVDAGSYVGGSLQPVTLATiykddllytyfnitdnqwLAMLMQQGTAQQKDT-- 233
Cdd:TIGR00999 77 LRSAReaKDGSYVEVRSPFDGYITQKSVTLGDYVAPQAELFRVAD------------------LGAVWVEAEVPAKDVsr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 234 --LPRQITVNLGEDgiQPYPATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIgTDQ 311
Cdd:TIGR00999 139 irKGSKATVLLENG--RPLPARVDYVGPEVDGSSRTAKVRVLIKNENLTLKPGLFVQVRVETKIGEPAIAVPEDAV-QDL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 189437920 312 LGKYVYVVNDSDRVRYRHIEVGQlIDDTLRQITGGLSPQERYVTR 356
Cdd:TIGR00999 216 GGRKVVFVRTQEGFRPRPVKVGR-RLGGYYEVLEGLKPGERVAVE 259
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
52-355 |
3.60e-18 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 84.83 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 52 GYLSSEKTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEA---ELNT----ARANLEYARNNYARML 124
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEAtlmELRAqrqqAEAELKLARVTLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 125 EAVKSDAVSQIQVLQSKSNVATSQAAVSN-------AEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVGGSLQPVT 197
Cdd:PRK11578 134 RLAKTQAVSQQDLDTAATELAVKQAQIGTidaqikrNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 198 LATIYKDDLLYTYFNITD----------NQWLAMLMQQGTA---QQKDTLPRQITVNlgeDGIQpypatldYFApnvdls 264
Cdd:PRK11578 214 ILTLADMSTMLVKAQVSEadvihlkpgqKAWFTVLGDPLTRyegVLKDILPTPEKVN---DAIF-------YYA------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 265 tgtlnlRARLDNPKGLLKSGLYVSITLPYGKESQAILIPDASIGtDQLGKYVYVVN--DSDRVRYRHIEVGqLIDDTLRQ 342
Cdd:PRK11578 278 ------RFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALG-DPVGDNRYKVKllRNGETREREVTIG-ARNDTDVE 349
|
330
....*....|...
gi 189437920 343 ITGGLSPQERYVT 355
Cdd:PRK11578 350 IVKGLEAGDEVII 362
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
52-198 |
2.51e-15 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 76.22 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 52 GYLSSEkTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANL------------------ 113
Cdd:PRK10476 42 AYIDAD-VVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQImttqrsvdaersnaasan 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 114 ---EYARNNY---ARMLE---------------------AVKSDAVSQIQVL-QSK------SNVATSQAAVSNAEAALN 159
Cdd:PRK10476 121 eqvERARANAklaTRTLErlepllakgyvsaqqvdqartAQRDAEVSLNQALlQAQaaaaavGGVDALVAQRAAREAALA 200
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 189437920 160 TARTNLGYCTVRAPFDGTVSRNQVDAGSYVgGSLQPV-TL 198
Cdd:PRK10476 201 IAELHLEDTTVRAPFDGRVVGLKVSVGEFA-APMQPIfTL 239
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
58-189 |
1.91e-11 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 64.60 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 58 KTVDLVARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANL------------------------ 113
Cdd:PRK03598 42 RTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLdlmlagyrdeeiaqaraavkqaqa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 114 --EYARNNYARMLEAVKSDAVSQIQVLQSKSN--------------------------VATSQAAVSNAEAALNTARTNL 165
Cdd:PRK03598 122 ayDYAQNFYNRQQGLWKSRTISANDLENARSSrdqaqatlksaqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNL 201
|
170 180
....*....|....*....|....
gi 189437920 166 GYCTVRAPFDGTVSRNQVDAGSYV 189
Cdd:PRK03598 202 QDTELIAPSDGTILTRAVEPGTML 225
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
59-189 |
6.36e-11 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 62.84 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 59 TVDLVA---RVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELNTARANLEYARNNYARMLEaVKSDAVSQI 135
Cdd:PRK10559 44 SADVVAiapDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNR-LGVQAMSRE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 189437920 136 QVLQSKSNVATSQAAVSNAEAALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYV 189
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFI 176
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
57-287 |
1.44e-09 |
|
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: 57.52 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 57 EKTVDLVARVNGTLQTI-AYAPGSRVRKGQVLFviepTIYQDNVKQTEAELNTARANLEYARNnyARMLEAvksdAVSQI 135
Cdd:pfam16576 17 RRLAHVHARVEGWIEKLyVNATGDPVKKGQPLA----ELYSPELVAAQQEYLLALRSGDALSK--SELLRA----ARQRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 136 QVLQsksnvatsqaaVSNAE-AALNTARTNLGYCTVRAPFDGTVSRNQVDAGSYVggslQP-VTLATIYKDDLLYTYFNI 213
Cdd:pfam16576 87 RLLG-----------MPEAQiAELERTGKVQPTVTVYAPISGVVTELNVREGMYV----QPgDTLFTIADLSTVWVEADV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189437920 214 TDNQwlAMLMQQGTaqqkdtlprQITVNLGEDGIQPYPATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLYV 287
Cdd:pfam16576 152 PEQD--LALVKVGQ---------PAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
169-284 |
6.26e-07 |
|
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: 47.36 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 169 TVRAPFDGTVSRNQVDAGSYVGgslQPVTLATIYKDD--LLYTYFNITDNQWLAMLMqqgtaqqkdtlprQITVNLGEDG 246
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQ---AGDPLATIVPPDrlLVEAFVPAADLGSLKKGQ-------------KVTLKLDPGS 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 189437920 247 IQPYPATLDYFAPNVDLSTGTLNLRARLDNPKG--LLKSG 284
Cdd:pfam13437 65 DYTLEGKVVRISPTVDPDTGVIPVRVSIENPKTpiPLLPG 104
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
64-107 |
4.81e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 40.50 E-value: 4.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 189437920 64 ARVNGTLQTIAYAPGSRVRKGQVLFVIEPTIYQDNVKQTEAELN 107
Cdd:pfam13533 7 SPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
98-165 |
2.34e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.72 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189437920 98 NVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNL 165
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNAL 151
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
98-165 |
1.58e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.04 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189437920 98 NVKQTEAELNTARANLEYARNNYARMLEAVKSDAVSQIQVLQSKSNVATSQAAVSNAEAALNTARTNL 165
Cdd:pfam02321 109 QLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLELLNAEADLELALAQL 176
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
169-358 |
2.74e-03 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 39.47 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 169 TVRAPFDGTVSRNQVDAGsyvggslqpvtlATIYKDDLLYTYFNItDNQWLAMLMQQGTAQQ-KDTLPRQITVNLGEDgi 247
Cdd:PRK09783 211 TLKAPIDGVITAFDLRAG------------MNIAKDNVVAKIQGM-DPVWVTAAIPESIAWLvKDASQFTLTVPARPD-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189437920 248 QPYPATLDYFAPNVDLSTGTLNLRARLDNPKGLLKSGLyvSITLPYGKESQA-ILIPDASI---GTDQlgkYVYVVNDSD 323
Cdd:PRK09783 276 KTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGM--NAWLQLNTASEPmLLIPSQALidtGSEQ---RVITVDADG 350
|
170 180 190
....*....|....*....|....*....|....*...
gi 189437920 324 RVRYRHIEVGQliddTLRQITG---GLSPQERYVTRAL 358
Cdd:PRK09783 351 RFVPKRVAVFQ----ESQGVTAirsGLAEGEKVVSSGL 384
|
|
| |
