|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-363 |
3.47e-73 |
|
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: 230.22 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 42 VKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADR 121
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 122 EFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSvVVKDSTVLAT 201
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQ-LVSAGTPLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 202 ITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGEFLRIRF 280
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPnPDGLLRPGMFVRVRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 281 MTAVDRGAWRVPQRCVKQLPDGTYsVFVMQ-DGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKAAA 359
Cdd:COG0845 242 VLGERENALLVPASAVVRDGGGAY-VFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVE 320
|
....
gi 512689015 360 KSSE 363
Cdd:COG0845 321 AAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
37-357 |
1.07e-54 |
|
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: 182.51 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 37 VDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEF 116
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 117 AQADREFQRAEKLWKAQAASQKDYDDAKS-LKNKTANeLAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVVKD 195
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAaVEAAQAD-LEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 196 STVlATITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGE 274
Cdd:TIGR01730 160 QTL-ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPnPDGRLLPGM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 275 FLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVMQDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTA 354
Cdd:TIGR01730 239 FGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAK 318
|
...
gi 512689015 355 VKA 357
Cdd:TIGR01730 319 VKV 321
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
2-357 |
4.76e-38 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 140.62 E-value: 4.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 2 NRTLVCCAAMSMFC-SLMLAGCKTQSSAPAPREPLPVDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIE 80
Cdd:PRK15030 4 NRGFTPLAVVLMLSgSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 81 GDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAA 160
Cdd:PRK15030 84 GSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 161 ENEARINLDWTAVRAPASGYVSKALFNPGSVVVK-DSTVLATITQKNDVRVLFAPSDRD-------LAGANIST---ATR 229
Cdd:PRK15030 164 VETARINLAYTKVTSPISGRIGKSNVTEGALVQNgQATALATVQQLDPIYVDVTQSSNDflrlkqeLANGTLKQengKAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 230 VRVFRASGEELPAS--LDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSV 306
Cdd:PRK15030 244 VSLITSDGIKFPQDgtLEFSDVTVDQTTGSITLRAIFPnPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATV 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 512689015 307 FVM-QDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKA 357
Cdd:PRK15030 324 LVVgADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKA 375
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
50-343 |
3.14e-25 |
|
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: 104.04 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 50 WLETIGQAEAAA-AVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADREFQRAEK 128
Cdd:pfam00529 7 GVEAPGRVVVSGnAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 129 LWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVVKDS-TVLATITQKND 207
Cdd:pfam00529 87 LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQaNLLATVAQLDQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 208 VRVLFAPSDRDLAGANISTATRVRVFRASGE-------------ELPASLD-YVAQ---TFDAKNGTRTMRAK--IPADS 268
Cdd:pfam00529 167 IYVQITQSAAENQAEVRSELSGAQLQIAEAEaelklakldlertEIRAPVDgTVAFlsvTVDGGTVSAGLRLMfvVPEDN 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512689015 269 GVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVM-QDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVIT 343
Cdd:pfam00529 247 LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVgISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-363 |
3.47e-73 |
|
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: 230.22 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 42 VKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADR 121
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 122 EFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSvVVKDSTVLAT 201
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQ-LVSAGTPLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 202 ITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGEFLRIRF 280
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPnPDGLLRPGMFVRVRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 281 MTAVDRGAWRVPQRCVKQLPDGTYsVFVMQ-DGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKAAA 359
Cdd:COG0845 242 VLGERENALLVPASAVVRDGGGAY-VFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVE 320
|
....
gi 512689015 360 KSSE 363
Cdd:COG0845 321 AAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
37-357 |
1.07e-54 |
|
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: 182.51 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 37 VDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEF 116
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 117 AQADREFQRAEKLWKAQAASQKDYDDAKS-LKNKTANeLAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVVKD 195
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAaVEAAQAD-LEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 196 STVlATITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGE 274
Cdd:TIGR01730 160 QTL-ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPnPDGRLLPGM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 275 FLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVMQDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTA 354
Cdd:TIGR01730 239 FGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAK 318
|
...
gi 512689015 355 VKA 357
Cdd:TIGR01730 319 VKV 321
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
2-357 |
4.76e-38 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 140.62 E-value: 4.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 2 NRTLVCCAAMSMFC-SLMLAGCKTQSSAPAPREPLPVDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIE 80
Cdd:PRK15030 4 NRGFTPLAVVLMLSgSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 81 GDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAA 160
Cdd:PRK15030 84 GSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 161 ENEARINLDWTAVRAPASGYVSKALFNPGSVVVK-DSTVLATITQKNDVRVLFAPSDRD-------LAGANIST---ATR 229
Cdd:PRK15030 164 VETARINLAYTKVTSPISGRIGKSNVTEGALVQNgQATALATVQQLDPIYVDVTQSSNDflrlkqeLANGTLKQengKAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 230 VRVFRASGEELPAS--LDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSV 306
Cdd:PRK15030 244 VSLITSDGIKFPQDgtLEFSDVTVDQTTGSITLRAIFPnPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATV 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 512689015 307 FVM-QDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKA 357
Cdd:PRK15030 324 LVVgADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKA 375
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
9-357 |
1.53e-34 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 130.68 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 9 AAMSMFCSLMLAGCKTQSSAPAPREPLPVDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGA 88
Cdd:PRK09578 10 LLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 89 VLFEIDPANLKTQ-------LASAEASRRAlevefaqADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAE 161
Cdd:PRK09578 90 VLFRIDPAPLKAArdaaagaLAKAEAAHLA-------ALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 162 NEARINLDWTAVRAPASGYVSKALFNPGSVVVKDS-TVLATITQKNDVRVLFAPSDRDLAGanISTATR----------- 229
Cdd:PRK09578 163 ARAQLQLDYATVTAPIDGRARRALVTEGALVGQDQaTPLTTVEQLDPIYVNFSQPAADVEA--LRRAVKsgratgiaqqd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 230 --VRVFRASGEE--LPASLDYVAQTFDAKNGTRTMRAKIP-ADSGVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTY 304
Cdd:PRK09578 241 vaVTLVRADGSEypLKGKLLFSDLAVDPTTDTVAMRALFPnPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSAS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 512689015 305 SVFVMQDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKA 357
Cdd:PRK09578 321 VKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKA 373
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
13-366 |
1.47e-31 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 122.90 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 13 MFCSLMLAGCKTQSSAPAPREPLPVDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFE 92
Cdd:PRK09859 12 LFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 93 IDPANLKTQLASAEASRRALEVEFAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTA 172
Cdd:PRK09859 92 IDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYAN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 173 VRAPASGYVSKALFNPGSVVVKD-STVLATITQKNDVRVLFAPSDRD-------LAGANI-----STATRVRVFRASGEE 239
Cdd:PRK09859 172 VTSPITGVSGKSSVTVGALVTANqADSLVTVQRLDPIYVDLTQSVQDflrmkeeVASGQIkqvqgSTPVQLNLENGKRYS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 240 LPASLDYVAQTFDAKNGTRTMRAKIPADSG-VLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVM-QDGKAIQK 317
Cdd:PRK09859 252 QTGTLKFSDPTVDETTGSVTLRAIFPNPNGdLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILdKDDVVQLR 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 512689015 318 AVEVGLWEGTDWIVTKGLADGDLVITNQLIKLQNGTAVKAAAkSSEKTA 366
Cdd:PRK09859 332 EIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAIS-SSQENA 379
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
34-366 |
1.45e-26 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 109.49 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 34 PLPVDIVAVKAADEAHWLETIGQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALE 113
Cdd:PRK11556 59 LAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 114 VEFAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVV 193
Cdd:PRK11556 139 ATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQIS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 194 K-DSTVLATITQKNDVRVLFAPSDRDLAganistatRVRVFRASGEELPA-----------------SLDyvaQTFDAKN 255
Cdd:PRK11556 219 SgDTTGIVVITQTHPIDLVFTLPESDIA--------TVVQAQKAGKPLVVeawdrtnskklsegtllSLD---NQIDATT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 256 GTRTMRAKIP-ADSGVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVMQDGKAIQKAVEVGLWEGTDWIVTKG 334
Cdd:PRK11556 288 GTIKLKARFNnQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAG 367
|
330 340 350
....*....|....*....|....*....|..
gi 512689015 335 LADGDLVITNQLIKLQNGTAVKAAAKSSEKTA 366
Cdd:PRK11556 368 LSAGDRVVTDGIDRLTEGAKVEVVEPQSATTP 399
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
50-343 |
3.14e-25 |
|
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: 104.04 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 50 WLETIGQAEAAA-AVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADREFQRAEK 128
Cdd:pfam00529 7 GVEAPGRVVVSGnAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 129 LWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVVKDS-TVLATITQKND 207
Cdd:pfam00529 87 LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQaNLLATVAQLDQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 208 VRVLFAPSDRDLAGANISTATRVRVFRASGE-------------ELPASLD-YVAQ---TFDAKNGTRTMRAK--IPADS 268
Cdd:pfam00529 167 IYVQITQSAAENQAEVRSELSGAQLQIAEAEaelklakldlertEIRAPVDgTVAFlsvTVDGGTVSAGLRLMfvVPEDN 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512689015 269 GVLPGEFLRIRFMTAVDRGAWRVPQRCVKQLPDGTYSVFVM-QDGKAIQKAVEVGLWEGTDWIVTKGLADGDLVIT 343
Cdd:pfam00529 247 LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVgISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
63-248 |
6.24e-22 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 95.11 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 63 VSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALE---------------------------VE 115
Cdd:COG1566 46 VTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEaqlarleaelgaeaeiaaaeaqlaaaqAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 116 FAQADREFQRAEKLWKAQAASQKDYDDAKSL---------------------------KNKTANELAQARAAENEARINL 168
Cdd:COG1566 126 LDLAQRELERYQALYKKGAVSQQELDEARAAldaaqaqleaaqaqlaqaqaglreeeeLAAAQAQVAQAEAALAQAELNL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 169 DWTAVRAPASGYVSKALFNPGSVVVKdSTVLATITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVA 248
Cdd:COG1566 206 ARTTIRAPVDGVVTNLNVEPGEVVSA-GQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSIS 284
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
71-199 |
2.17e-14 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 73.07 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 71 GRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFA--------------------------QADREFQ 124
Cdd:PRK03598 52 GRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkqaqaaydYAQNFYN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 125 RAEKLWKAQAASQKDYDDAKSLKN------KTANE--------------------LAQARAAENEARINLDWTAVRAPAS 178
Cdd:PRK03598 132 RQQGLWKSRTISANDLENARSSRDqaqatlKSAQDklsqyregnrpqdiaqakasLAQAQAALAQAELNLQDTELIAPSD 211
|
170 180
....*....|....*....|.
gi 512689015 179 GYVSKALFNPGSVVVKDSTVL 199
Cdd:PRK03598 212 GTILTRAVEPGTMLNAGSTVF 232
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
59-254 |
8.50e-12 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 65.15 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 59 AAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADREFQRAEKLwKAQAASQK 138
Cdd:PRK10559 44 SADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 139 DYDDAKSLKNKTANELAQARAAENEARINLDWTAVRAPASGYVSKALFNPGSVVVKDSTVLATItQKNDVRVLFAPSDRD 218
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALV-KQNSFYVLAYMEETK 201
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512689015 219 LAG------ANISTATRVRVFRASGEELPASLDYVAQTFDAK 254
Cdd:PRK10559 202 LEGvrpgyrAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSK 243
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
55-343 |
9.55e-10 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 59.40 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 55 GQAEAAAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEASRRALEVEFAQADRE-------FQRAE 127
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAElklarvtLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 128 KLWKAQAASQKDYDDAKS----LKNKTANELAQ---ARAAENEARINLDWTAVRAPASGYVSK----------------- 183
Cdd:PRK11578 134 RLAKTQAVSQQDLDTAATelavKQAQIGTIDAQikrNQASLDTAKTNLDYTRIVAPMAGEVTQittlqgqtviaaqqapn 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 184 --ALFNPGSVVVKDSTVLATIT-----QKNDVRVLFAPSDRdlaganisTATRVRVFRASGEELPASLDYVAQtFDAKNG 256
Cdd:PRK11578 214 ilTLADMSTMLVKAQVSEADVIhlkpgQKAWFTVLGDPLTR--------YEGVLKDILPTPEKVNDAIFYYAR-FEVPNP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 257 TRTMRAKIPADSGVLPGEFLRIRFMTAVDRGawrvpqrcvKQLPDGTYSVFVMQDGKAIQKAVEVGLWEGTDWIVTKGLA 336
Cdd:PRK11578 285 NGLLRLDMTAQVHIQLTDVKNVLTIPLSALG---------DPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLE 355
|
....*..
gi 512689015 337 DGDLVIT 343
Cdd:PRK11578 356 AGDEVII 362
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
65-277 |
6.12e-08 |
|
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: 52.51 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 65 VTTQATGRIiaQR-YI--EGDFVEAGAVLFEIDpanlKTQLASAEAsrralevEFAQADREFQRAEKLWKAQAASQKdyd 141
Cdd:pfam16576 22 VHARVEGWI--EKlYVnaTGDPVKKGQPLAELY----SPELVAAQQ-------EYLLALRSGDALSKSELLRAARQR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 142 daksLKN-----KTANELAQARaaenEARINLdwtAVRAPASGYVSKALFNPGSVVvKDSTVLATITQKNDVRVLFAPSD 216
Cdd:pfam16576 86 ----LRLlgmpeAQIAELERTG----KVQPTV---TVYAPISGVVTELNVREGMYV-QPGDTLFTIADLSTVWVEADVPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512689015 217 RDLAGANISTATRVRVFRASGEELPASLDYVAQTFDAKngTRTMRAKIPADSgvlPGEFLR 277
Cdd:pfam16576 154 QDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPK--TRTVRVRIELPN---PDGRLK 209
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
60-202 |
1.98e-07 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 52.34 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 60 AAAVSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEAS-----------RRALEVE------------- 115
Cdd:PRK10476 46 ADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADlaladaqimttQRSVDAErsnaasaneqver 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 116 ----FAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQAR------------------------AAENEARIN 167
Cdd:PRK10476 126 aranAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALlqaqaaaaavggvdalvaqraareAALAIAELH 205
|
170 180 190
....*....|....*....|....*....|....*
gi 512689015 168 LDWTAVRAPASGYVSKALFNPGSVVVKDSTVLATI 202
Cdd:PRK10476 206 LEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI 240
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
173-272 |
3.47e-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: 48.13 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 173 VRAPASGYVSKALFNPGSVVVKDsTVLATITQKNDVRVLFAPSDRDLAGANISTATRVRVFRASGEELPASLDYVAQTFD 252
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAG-DPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|
gi 512689015 253 AKNGTRTMRAKIPADSGVLP 272
Cdd:pfam13437 81 PDTGVIPVRVSIENPKTPIP 100
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
63-107 |
6.83e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 40.12 E-value: 6.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 512689015 63 VSVTTQATGRIIAQRYIEGDFVEAGAVLFEIDPANLKTQLASAEA 107
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
74-164 |
4.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689015 74 IAQRY------IEgdfvEAGAVLFEiDPANLKTQLASAEASRRALEVEFAQADREFQRAEKL---WKAQAASQKDYDDak 144
Cdd:PRK00409 493 IAKRLglpeniIE----EAKKLIGE-DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEED-- 565
|
90 100
....*....|....*....|.
gi 512689015 145 SLKNKTANELAQA-RAAENEA 164
Cdd:PRK00409 566 KLLEEAEKEAQQAiKEAKKEA 586
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
101-168 |
8.21e-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: 37.12 E-value: 8.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512689015 101 QLASAEASRRALEVEFAQADREFQRAEKLWKAQAASQKDYDDAKSLKNKTANELAQARAAENEARINL 168
Cdd:pfam02321 109 QLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLELLNAEADLELALAQL 176
|
|
| |
