|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
12-369 |
2.74e-113 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 335.92 E-value: 2.74e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 12 LLLSGCDNTQSNNSSPSETEVGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAA 91
Cdd:PRK15030 20 LALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 92 SYQAAWNEARAALQQAQALVKADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAP 171
Cdd:PRK15030 100 TYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 172 ISGRIGISSVTPGALVTASQDTALTTIRGLDTMYVDLTRSSVDLLRLRKQ----SLATNSDTMSVSLILEDGTTYSEKGR 247
Cdd:PRK15030 180 ISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQElangTLKQENGKAKVSLITSDGIKFPQDGT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 248 LELTEVAVDESTGSVTLRAIFPNPQQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLET 327
Cdd:PRK15030 260 LEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVA 339
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15831117 328 GETYGDKWLVLNGLHSGDRLIVEGSAKVTSGQTVKAVEVQAN 369
Cdd:PRK15030 340 SQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTAD 381
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
36-368 |
2.92e-86 |
|
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: 264.11 E-value: 2.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 36 TVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADC 115
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 116 QKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQdtAL 195
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 196 TTIRGLDTMYVDLTRSSVDLLRLRKQslatnsdtMSVSLILEDGTTYSEKGRLELTEVAVDESTGSVTLRAIFPNPQQQL 275
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVG--------QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 276 LPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNaTALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRLIVEGSAKV 355
Cdd:COG0845 232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGA-YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRL 310
|
330
....*....|...
gi 15831117 356 TSGQTVKAVEVQA 368
Cdd:COG0845 311 RDGAKVRVVEAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
32-364 |
4.41e-74 |
|
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: 232.59 E-value: 4.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 32 VGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALV 111
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 112 KADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTAsq 191
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 192 DTALTTIRGLDTMYVDLTRSSVDLLRLRKqslatnSDTMSVSLILEDGTTYseKGRLELTEVAVDESTGSVTLRAIFPNP 271
Cdd:TIGR01730 159 GQTLATIVDLDPLEADFSVPERDLPQLRR------GQTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRATFPNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 272 QQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNAtALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRLIVEG 351
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKY-VYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAG 309
|
330
....*....|...
gi 15831117 352 SAKVTSGQTVKAV 364
Cdd:TIGR01730 310 VVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
39-349 |
4.98e-55 |
|
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: 183.39 E-value: 4.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 39 SQPVSVVSELTGRTSAALSAE-VRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADCQK 117
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 118 AQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQDTALTT 197
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 198 IRGLDTMYVDLTRSSVDLLRLRKQSLATNSDTMS-----VSLILEDGTTYSEK----GRLELTEVAVDESTGSVTLRAIF 268
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAeaeaeLKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 269 PNPQQQLL-PGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRL 347
Cdd:pfam00529 241 VVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 15831117 348 IV 349
Cdd:pfam00529 321 RL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
12-369 |
2.74e-113 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 335.92 E-value: 2.74e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 12 LLLSGCDNTQSNNSSPSETEVGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAA 91
Cdd:PRK15030 20 LALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 92 SYQAAWNEARAALQQAQALVKADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAP 171
Cdd:PRK15030 100 TYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 172 ISGRIGISSVTPGALVTASQDTALTTIRGLDTMYVDLTRSSVDLLRLRKQ----SLATNSDTMSVSLILEDGTTYSEKGR 247
Cdd:PRK15030 180 ISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQElangTLKQENGKAKVSLITSDGIKFPQDGT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 248 LELTEVAVDESTGSVTLRAIFPNPQQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLET 327
Cdd:PRK15030 260 LEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVA 339
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15831117 328 GETYGDKWLVLNGLHSGDRLIVEGSAKVTSGQTVKAVEVQAN 369
Cdd:PRK15030 340 SQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTAD 381
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
13-369 |
6.12e-98 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 296.24 E-value: 6.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 13 LLSGCDNTQSNNSSPSETEVGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAAS 92
Cdd:PRK09859 17 MLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 93 YQAAWNEARAALQQAQALVKADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPI 172
Cdd:PRK09859 97 LQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 173 SGRIGISSVTPGALVTASQDTALTTIRGLDTMYVDLTRSSVDLLRLRKQ----SLATNSDTMSVSLILEDGTTYSEKGRL 248
Cdd:PRK09859 177 TGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEvasgQIKQVQGSTPVQLNLENGKRYSQTGTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 249 ELTEVAVDESTGSVTLRAIFPNPQQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLETG 328
Cdd:PRK09859 257 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEAS 336
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15831117 329 ETYGDKWLVLNGLHSGDRLIVEGSAKVTSGQTVKAVEVQAN 369
Cdd:PRK09859 337 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQE 377
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
36-368 |
2.92e-86 |
|
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: 264.11 E-value: 2.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 36 TVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADC 115
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 116 QKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQdtAL 195
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 196 TTIRGLDTMYVDLTRSSVDLLRLRKQslatnsdtMSVSLILEDGTTYSEKGRLELTEVAVDESTGSVTLRAIFPNPQQQL 275
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVG--------QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 276 LPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNaTALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRLIVEGSAKV 355
Cdd:COG0845 232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGA-YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRL 310
|
330
....*....|...
gi 15831117 356 TSGQTVKAVEVQA 368
Cdd:COG0845 311 RDGAKVRVVEAAA 323
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
2-373 |
4.64e-81 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 252.79 E-value: 4.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 2 KYIATSVVAMLLLSGCDNTQSNNSSPSETEVGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKA 81
Cdd:PRK09578 8 RLLLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 82 GQPLYQIDAASYQAAWNEARAALQQAQALVKADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARI 161
Cdd:PRK09578 88 GAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 162 NLDWTTVTAPISGRIGISSVTPGALVTASQDTALTTIRGLDTMYVDLTRSSVDLLRLRK-----QSLATNSDTMSVSLIL 236
Cdd:PRK09578 168 QLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRavksgRATGIAQQDVAVTLVR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 237 EDGTTYSEKGRLELTEVAVDESTGSVTLRAIFPNPQQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAkGNATALVVNK 316
Cdd:PRK09578 248 ADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTA-DSASVKVVGQ 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831117 317 DNKVEQRTLETGETYGDKWLVLNGLHSGDRLIVEGSAKVTSGQTVKAVEVQANGGNA 373
Cdd:PRK09578 327 NGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAAKPA 383
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
32-364 |
4.41e-74 |
|
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: 232.59 E-value: 4.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 32 VGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALV 111
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 112 KADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTAsq 191
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 192 DTALTTIRGLDTMYVDLTRSSVDLLRLRKqslatnSDTMSVSLILEDGTTYseKGRLELTEVAVDESTGSVTLRAIFPNP 271
Cdd:TIGR01730 159 GQTLATIVDLDPLEADFSVPERDLPQLRR------GQTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRATFPNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 272 QQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNAtALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRLIVEG 351
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKY-VYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAG 309
|
330
....*....|...
gi 15831117 352 SAKVTSGQTVKAV 364
Cdd:TIGR01730 310 VVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
39-349 |
4.98e-55 |
|
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: 183.39 E-value: 4.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 39 SQPVSVVSELTGRTSAALSAE-VRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADCQK 117
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 118 AQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQDTALTT 197
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 198 IRGLDTMYVDLTRSSVDLLRLRKQSLATNSDTMS-----VSLILEDGTTYSEK----GRLELTEVAVDESTGSVTLRAIF 268
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAeaeaeLKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 269 PNPQQQLL-PGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRL 347
Cdd:pfam00529 241 VVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 15831117 348 IV 349
Cdd:pfam00529 321 RL 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
32-368 |
5.97e-35 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 132.61 E-value: 5.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 32 VGVVTVKSQPVSVVSELTGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALV 111
Cdd:PRK11556 62 VQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 112 KADCQKAQRYARLVKENGVSQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQ 191
Cdd:PRK11556 142 ANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 192 DTALTTIRglDTMYVDLtrssvdLLRLRKQSLAT------NSDTMSVSLILEDGTTYSEKGRLELTEVAVDESTGSVTLR 265
Cdd:PRK11556 222 TTGIVVIT--QTHPIDL------VFTLPESDIATvvqaqkAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 266 AIFPNPQQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATaLVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGD 345
Cdd:PRK11556 294 ARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFV-WVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGD 372
|
330 340
....*....|....*....|...
gi 15831117 346 RLIVEGSAKVTSGQTVKAVEVQA 368
Cdd:PRK11556 373 RVVTDGIDRLTEGAKVEVVEPQS 395
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-288 |
8.71e-17 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 80.48 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 2 KYIATSVVAMLLLSGCDNTQSNNSSPSETEVGVVTVKSQPVSvvseltgrtsaalsaevrPQVGGIIQKRLFKEGDLVKA 81
Cdd:COG1566 8 RLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVA------------------AKVSGRVTEVLVKEGDRVKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 82 GQPLYQIDAASYQAA-----------------------WNEARAALQQAQALVKADCQKAQ----RYARLVKENGVSQQD 134
Cdd:COG1566 70 GQVLARLDPTDLQAAlaqaeaqlaaaeaqlarleaelgAEAEIAAAEAQLAAAQAQLDLAQreleRYQALYKKGAVSQQE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 135 ADDAQ---------------------------STCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALV 187
Cdd:COG1566 150 LDEARaaldaaqaqleaaqaqlaqaqaglreeEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 188 TASQdtALTTIRGLDTMYVDLTRSSVDLLRLRKQSLATnsdtmsVSLILEDGTTYseKGRLE------LTEVAVDESTGS 261
Cdd:COG1566 230 SAGQ--PLLTIVPLDDLWVEAYVPETDLGRVKPGQPVE------VRVDAYPDRVF--EGKVTsispgaGFTSPPKNATGN 299
|
330 340 350
....*....|....*....|....*....|..
gi 15831117 262 VTLR-----AIFPNPQQQLLPGMFVRARVDEG 288
Cdd:COG1566 300 VVQRypvriRLDNPDPEPLRPGMSATVEIDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
49-349 |
4.15e-11 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 63.64 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 49 TGRTSAALSAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQ-------AAWNEARAALQQAQALVKADCQKAQRY 121
Cdd:PRK11578 53 TGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLMELRAQRQQAEAELKLARVTLSRQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 122 ARLVKENGVSQQDADDA-------QSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVTASQDTA 194
Cdd:PRK11578 133 QRLAKTQAVSQQDLDTAatelavkQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 195 -LTTIRGLDTMYVDLTRSSVDLLRLRKQSLAtnsdtmSVSLILEDGTTYSekGRLELTEVAVDESTGSVTLRAIF--PNP 271
Cdd:PRK11578 213 nILTLADMSTMLVKAQVSEADVIHLKPGQKA------WFTVLGDPLTRYE--GVLKDILPTPEKVNDAIFYYARFevPNP 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831117 272 QQQLLPGMFVRARVDEGVMEDAILAPQQGVTRDAKGNATALVVNKDNKVEQRTLETGETYGDKWLVLNGLHSGDRLIV 349
Cdd:PRK11578 285 NGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
60-281 |
1.68e-05 |
|
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: 45.19 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 60 VRPQVGGIIQKrLF--KEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADCQKAQRyARLvKENGVSQQDADd 137
Cdd:pfam16576 22 VHARVEGWIEK-LYvnATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKSELLRAAR-QRL-RLLGMPEAQIA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 138 aqstcaqdkasvaakkaALETARINLDWTTVTAPISGRIGISSVTPGALVTASQdtALTTIRGLDTMYVDltrssVDLLr 217
Cdd:pfam16576 98 -----------------ELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGD--TLFTIADLSTVWVE-----ADVP- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831117 218 lrKQSLATNSDTMSVSLILE--DGTTYseKGRLELTEVAVDESTGSVTLRAIFPNPQQQLLPGMFV 281
Cdd:pfam16576 153 --EQDLALVKVGQPAEVTLPalPGKTF--EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
64-196 |
1.01e-04 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 43.80 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 64 VGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQAL---------------VKADCQKAQ---RYA--- 122
Cdd:PRK03598 50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQldlmlagyrdeeiaqARAAVKQAQaayDYAqnf 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 123 -----RLVKENGVSQQDADDAQSTCAQDKASVAAKKAALE--------------------------TARINLDWTTVTAP 171
Cdd:PRK03598 130 ynrqqGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSqyregnrpqdiaqakaslaqaqaalaQAELNLQDTELIAP 209
|
170 180
....*....|....*....|....*
gi 15831117 172 ISGRIGISSVTPGALVtASQDTALT 196
Cdd:PRK03598 210 SDGTILTRAVEPGTML-NAGSTVFT 233
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
57-96 |
1.65e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 38.96 E-value: 1.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15831117 57 SAEVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAA 96
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQ 41
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
54-188 |
1.70e-04 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 43.19 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 54 AALSAEV---RPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNEARAALQQAQALVKADCQKAQRYARLvKENGV 130
Cdd:PRK10559 41 ARFSADVvaiAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAM 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831117 131 SQQDADDAQSTCAQDKASVAAKKAALETARINLDWTTVTAPISGRIGISSVTPGALVT 188
Cdd:PRK10559 120 SREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFIT 177
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
53-191 |
2.13e-04 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 42.71 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 53 SAALSAE---VRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAAWNE-----------------ARAALQQAQALVK 112
Cdd:PRK10476 41 DAYIDADvvhVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQaqadlaladaqimttqrSVDAERSNAASAN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 113 ADCQKAQ-----------RYARLVKENGVSQQDADDAQ------------------------STCAQDKASVAAKKAALE 157
Cdd:PRK10476 121 EQVERARanaklatrtleRLEPLLAKGYVSAQQVDQARtaqrdaevslnqallqaqaaaaavGGVDALVAQRAAREAALA 200
|
170 180 190
....*....|....*....|....*....|....
gi 15831117 158 TARINLDWTTVTAPISGRIGISSVTPGALVTASQ 191
Cdd:PRK10476 201 IAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQ 234
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
167-278 |
2.29e-04 |
|
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: 40.04 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831117 167 TVTAPISGRIGISSVTPGALVTASQdtALTTIRGLDTMYVDLTRSSVDLLRLRKQslatnsdtMSVSLILEDGTTYSEKG 246
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGD--PLATIVPPDRLLVEAFVPAADLGSLKKG--------QKVTLKLDPGSDYTLEG 70
|
90 100 110
....*....|....*....|....*....|....
gi 15831117 247 RLELTEVAVDESTGSVTLRAIFPNP--QQQLLPG 278
Cdd:pfam13437 71 KVVRISPTVDPDTGVIPVRVSIENPktPIPLLPG 104
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
59-96 |
4.58e-04 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 41.92 E-value: 4.58e-04
10 20 30
....*....|....*....|....*....|....*...
gi 15831117 59 EVRPQVGGIIQKRLFKEGDLVKAGQPLYQIDAASYQAA 96
Cdd:TIGR01843 45 VVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEAD 82
|
|
| |
