|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
1-374 |
3.33e-179 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 503.86 E-value: 3.33e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 1 MTKHARFSLLPSFIIFSAAL-LAGCNDQGDTQAHAGEPQVTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRN 79
Cdd:PRK15030 1 MNKNRGFTPLAVVLMLSGSLaLTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 80 FTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAA 159
Cdd:PRK15030 81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 160 KAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQSTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKDSA 239
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 240 SSTVQLVMENGQVYPIKGTLQFSDVTVDESTGSITLRAVFPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGD 319
Cdd:PRK15030 241 KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446082528 320 AMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKVIVSGLQKARPGVQVKA 374
Cdd:PRK15030 321 ATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKA 375
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
44-380 |
8.19e-95 |
|
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: 286.45 E-value: 8.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 44 VETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHL 123
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 124 TVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQstELA 203
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 204 TVQQLDPIYVDVTQSSNDFMRLKQsveqgnlhkdsaSSTVQLVMENGQVYPIKGTLQFSDVTVDESTGSITLRAVFPNPQ 283
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARLKV------------GQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 284 HSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAmVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKVIVSGL 363
Cdd:COG0845 229 GLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAY-VFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGL 307
|
330
....*....|....*..
gi 446082528 364 QKARPGVQVKATTDAPA 380
Cdd:COG0845 308 QRLRDGAKVRVVEAAAP 324
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
46-360 |
3.94e-80 |
|
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: 248.88 E-value: 3.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 46 TAPLAVTTELPGRTSAFRIAE-VRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLT 124
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 125 VKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQSTELAT 204
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 205 VQQLDPIYVDVTQSSNDFMRL-KQSVEQGNLHKDSASSTVQLVMENGQVYPIK----GTLQFSDVTVDESTGSITLRAVF 279
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 280 PNPQHSLL-PGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKV 358
Cdd:pfam00529 241 VVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 446082528 359 IV 360
Cdd:pfam00529 321 RL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
39-375 |
1.44e-78 |
|
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: 244.53 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 39 VTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAA 118
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 119 AIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQ 198
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 199 stELATVQQLDPIYVDVTQSSNDFMRLKQSVEqgnlhkdsasSTVQLVMENGQVYpiKGTLQFSDVTVDESTGSITLRAV 278
Cdd:TIGR01730 161 --TLATIVDLDPLEADFSVPERDLPQLRRGQT----------LTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 279 FPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDaMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKV 358
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGK-YVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 446082528 359 IVSGLQKARPGVQVKAT 375
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
1-374 |
3.33e-179 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 503.86 E-value: 3.33e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 1 MTKHARFSLLPSFIIFSAAL-LAGCNDQGDTQAHAGEPQVTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRN 79
Cdd:PRK15030 1 MNKNRGFTPLAVVLMLSGSLaLTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 80 FTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAA 159
Cdd:PRK15030 81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 160 KAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQSTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKDSA 239
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 240 SSTVQLVMENGQVYPIKGTLQFSDVTVDESTGSITLRAVFPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGD 319
Cdd:PRK15030 241 KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446082528 320 AMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKVIVSGLQKARPGVQVKA 374
Cdd:PRK15030 321 ATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKA 375
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
9-376 |
7.24e-124 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 362.88 E-value: 7.24e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 9 LLPsfIIFSAALLAGCNDQGDTQAHAGEPQVTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEA 88
Cdd:PRK09859 8 LIP--LLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 89 GQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARI 168
Cdd:PRK09859 86 GDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 169 NLAYTKVTSPISGRIGKSNVTEGALVTNGQSTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKDSASSTVQLVME 248
Cdd:PRK09859 166 NLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 249 NGQVYPIKGTLQFSDVTVDESTGSITLRAVFPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAMVMVVNDK 328
Cdd:PRK09859 246 NGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446082528 329 SQVEARNVVAAQAIGDKWLISEGLKPGDKVIVSGLQKARPGVQVKATT 376
Cdd:PRK09859 326 DVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAIS 373
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
13-385 |
6.23e-99 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 299.02 E-value: 6.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 13 FIIFSAALLAGCNDQGDTQAHAGEPQVTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSL 92
Cdd:PRK09578 12 AALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 93 YQIDPATYQADYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAY 172
Cdd:PRK09578 92 FRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 173 TKVTSPISGRIGKSNVTEGALVTNGQSTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLH-KDSASSTVQLVMENGQ 251
Cdd:PRK09578 172 ATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATgIAQQDVAVTLVRADGS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 252 VYPIKGTLQFSDVTVDESTGSITLRAVFPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPrGDAMVMVVNDKSQV 331
Cdd:PRK09578 252 EYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTA-DSASVKVVGQNGKV 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446082528 332 EARNVVAAQAIGDKWLISEGLKPGDKVIVSGLQKARPGVQVKATTDAPAAKTAQ 385
Cdd:PRK09578 331 RDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAAKPAP 384
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
44-380 |
8.19e-95 |
|
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: 286.45 E-value: 8.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 44 VETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHL 123
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 124 TVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQstELA 203
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 204 TVQQLDPIYVDVTQSSNDFMRLKQsveqgnlhkdsaSSTVQLVMENGQVYPIKGTLQFSDVTVDESTGSITLRAVFPNPQ 283
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARLKV------------GQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 284 HSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAmVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKVIVSGL 363
Cdd:COG0845 229 GLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAY-VFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGL 307
|
330
....*....|....*..
gi 446082528 364 QKARPGVQVKATTDAPA 380
Cdd:COG0845 308 QRLRDGAKVRVVEAAAP 324
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
46-360 |
3.94e-80 |
|
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: 248.88 E-value: 3.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 46 TAPLAVTTELPGRTSAFRIAE-VRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLT 124
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 125 VKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQSTELAT 204
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 205 VQQLDPIYVDVTQSSNDFMRL-KQSVEQGNLHKDSASSTVQLVMENGQVYPIK----GTLQFSDVTVDESTGSITLRAVF 279
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 280 PNPQHSLL-PGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKV 358
Cdd:pfam00529 241 VVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 446082528 359 IV 360
Cdd:pfam00529 321 RL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
39-375 |
1.44e-78 |
|
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: 244.53 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 39 VTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAA 118
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 119 AIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQ 198
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 199 stELATVQQLDPIYVDVTQSSNDFMRLKQSVEqgnlhkdsasSTVQLVMENGQVYpiKGTLQFSDVTVDESTGSITLRAV 278
Cdd:TIGR01730 161 --TLATIVDLDPLEADFSVPERDLPQLRRGQT----------LTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 279 FPNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDaMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKV 358
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGK-YVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 446082528 359 IVSGLQKARPGVQVKAT 375
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
47-384 |
1.63e-40 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 148.01 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 47 APLAVTTELP------GRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAI 120
Cdd:PRK11556 64 AATATEQAVPryltglGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLAN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 121 AHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQST 200
Cdd:PRK11556 144 ARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 201 ELATVQQLDPIYVDVTQSSNDFMRLKQSveqgnlHKDSASSTVQLVMENGQVYPIKGTLQFSDVTVDESTGSITLRAVFP 280
Cdd:PRK11556 224 GIVVITQTHPIDLVFTLPESDIATVVQA------QKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 281 NPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDaMVMVVNDKSQVEARNVVAAQAIGDKWLISEGLKPGDKVIV 360
Cdd:PRK11556 298 NQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGH-FVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVT 376
|
330 340
....*....|....*....|....*...
gi 446082528 361 SGLQKARPGVQVK----ATTDAPAAKTA 384
Cdd:PRK11556 377 DGIDRLTEGAKVEvvepQSATTPEEKAT 404
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
57-299 |
3.36e-17 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 81.63 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 57 GRTSAfRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELAKSEAAAAIAHLTV----------- 125
Cdd:COG1566 39 GRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELgaeaeiaaaea 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 126 ----------------KRYVPLVGTKYISQQEYDQA---------------------------IADARQADAAVVAAKAA 162
Cdd:COG1566 118 qlaaaqaqldlaqrelERYQALYKKGAVSQQELDEAraaldaaqaqleaaqaqlaqaqaglreEEELAAAQAQVAQAEAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 163 VESARINLAYTKVTSPISGRIGKSNVTEGALVTNGQSteLATVQQLDPIYVDVTQSSND--FMRLKQSVEqgnlhkdsas 240
Cdd:COG1566 198 LAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDlgRVKPGQPVE---------- 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 241 stVQLVMENGQVYpiKGTLQF------SDVTVDESTGSITL----RAVFPNPQ-HSLLPGMFVRARIDEG 299
Cdd:COG1566 266 --VRVDAYPDRVF--EGKVTSispgagFTSPPKNATGNVVQrypvRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
48-292 |
4.68e-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: 55.98 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 48 PLAVTTELPGRTSA--FRIAEVRPQVSGIV--LKRNFTeGSDVEAGQSLYQI---DPATYQADYDSAKgELAKSEAAAAI 120
Cdd:pfam16576 1 PLSRTIRAVGRVAYdeRRLAHVHARVEGWIekLYVNAT-GDPVKKGQPLAELyspELVAAQQEYLLAL-RSGDALSKSEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 121 AHLTVKRYVPL-VGTKYISQQEYDQAIadarqadaavvaakaavesaRINLAytkVTSPISGRIGKSNVTEGALVTNGQs 199
Cdd:pfam16576 79 LRAARQRLRLLgMPEAQIAELERTGKV--------------------QPTVT---VYAPISGVVTELNVREGMYVQPGD- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 200 tELATVQQLDP--IYVDVTQSSNDFMRLKQSVEqgnlhkdsasstVQLVMENGQVYpiKGTLQFSDVTVDESTGSITLRA 277
Cdd:pfam16576 135 -TLFTIADLSTvwVEADVPEQDLALVKVGQPAE------------VTLPALPGKTF--EGKVDYIYPTLDPKTRTVRVRI 199
|
250
....*....|....*
gi 446082528 278 VFPNPQHSLLPGMFV 292
Cdd:pfam16576 200 ELPNPDGRLKPGMFA 214
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
33-361 |
1.05e-07 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 53.24 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 33 HAGEPQVTVHVVETAPLAVTTELPGRTSAFRIAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQ-------ADYD 105
Cdd:PRK11578 30 NAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 106 SAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVVA-------AKAAVESARINLAYTKVTSP 178
Cdd:PRK11578 110 ELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQIGTidaqikrNQASLDTAKTNLDYTRIVAP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 179 ISGRIGKSNVTEGALVTNGQ-STELATVQQLDPIYVDVTQSSNDFMRLKQSVEqgnlhkdsASSTVqlVMENGQVYPikG 257
Cdd:PRK11578 190 MAGEVTQITTLQGQTVIAAQqAPNILTLADMSTMLVKAQVSEADVIHLKPGQK--------AWFTV--LGDPLTRYE--G 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 258 TLQFSDVTVDESTGSITLRAVF--PNPQHSLLPGMFVRARIDEGVQPNAILVPQQGVTRTPRGDAMVMVVNDKSQVEARN 335
Cdd:PRK11578 258 VLKDILPTPEKVNDAIFYYARFevPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGDNRYKVKLLRNGETRERE 337
|
330 340
....*....|....*....|....*.
gi 446082528 336 VVAAQAIGDKWLISEGLKPGDKVIVS 361
Cdd:PRK11578 338 VTIGARNDTDVEIVKGLEAGDEVIIG 363
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
167-363 |
1.71e-06 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 49.48 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 167 RINLAYTkVTSPISGRIGKSNVTEGALVTngQSTELATVQQLDPIYVDVTqssndfmrLKQSVEQgnLHKDSASSTVQLV 246
Cdd:PRK09783 205 KIQTRFT-LKAPIDGVITAFDLRAGMNIA--KDNVVAKIQGMDPVWVTAA--------IPESIAW--LVKDASQFTLTVP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 247 MENGQVYPI-KGTLQFSdvtVDESTGSITLRAVFPNPQHSLLPGMFVRARIDEGVQPnAILVPQQGVTRTPRGDAMVMVV 325
Cdd:PRK09783 272 ARPDKTFTIrKWTLLPS---VDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEP-MLLIPSQALIDTGSEQRVITVD 347
|
170 180 190
....*....|....*....|....*....|....*...
gi 446082528 326 NDKSQVEARNVVAAQAIGDKwLISEGLKPGDKVIVSGL 363
Cdd:PRK09783 348 ADGRFVPKRVAVFQESQGVT-AIRSGLAEGEKVVSSGL 384
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
39-213 |
2.31e-06 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 48.97 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 39 VTVHVVETAPLAVT------TELP----GRTSAFRIAeVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAK 108
Cdd:PRK10559 13 ITLVLVILAFIAIFrawvfyTESPwtrdARFSADVVA-IAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 109 GELAKSEAAAAIAHLTVKRYVPLvGTKYISQQEYDQAIADARQADAAVVAAKAAVESARINLAYTKVTSPISGRIGKSNV 188
Cdd:PRK10559 92 ADVAYYQVLAQEKRREAGRRNRL-GVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNV 170
|
170 180
....*....|....*....|....*
gi 446082528 189 TEGALVTNGqSTELATVQQlDPIYV 213
Cdd:PRK10559 171 YTGEFITRG-STAVALVKQ-NSFYV 193
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
174-289 |
3.63e-05 |
|
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: 42.35 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 174 KVTSPISGRIGKSNVTEGALVTNGQstELATVQQLDPIYVDVTQSSNDFmrlkQSVEQGnlhkdsasSTVQLVMENGQVY 253
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGD--PLATIVPPDRLLVEAFVPAADL----GSLKKG--------QKVTLKLDPGSDY 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 446082528 254 PIKGTLQFSDVTVDESTGSITLRAVFPNPQHS--LLPG 289
Cdd:pfam13437 67 TLEGKVVRISPTVDPDTGVIPVRVSIENPKTPipLLPG 104
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
65-112 |
4.93e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.42 E-value: 4.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446082528 65 AEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELA 112
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
64-145 |
6.27e-04 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 41.55 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082528 64 IAEVRPQVSGIVLKRNFTEGSDVEAGQSLYQIDPATYQADYDSAKGELA----------------------------KSE 115
Cdd:PRK10476 48 VVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladaqimttqrsvdaersnaasaneqveRAR 127
|
90 100 110
....*....|....*....|....*....|
gi 446082528 116 AAAAIAHLTVKRYVPLVGTKYISQQEYDQA 145
Cdd:PRK10476 128 ANAKLATRTLERLEPLLAKGYVSAQQVDQA 157
|
|
| |
