|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
4-284 |
4.89e-76 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 234.25 E-value: 4.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 4 KTLKYFSTLFVLVLALIAGWWLWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIA 83
Cdd:PRK10559 7 KISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 84 VLNAQAQLAKAQSDLAKANNEANRRRHLSQNYISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVT 163
Cdd:PRK10559 87 LAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 164 NLSARVGNYATTGQPVFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGSQTLQGHVSSIGRAIYDQSVETDSGLVP 243
Cdd:PRK10559 167 NLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1278866364 244 DIKPNVPWVRLAQRVPVRVEFDRLPeGITLVSGTTCTVSIG 284
Cdd:PRK10559 247 TIDSNLEWVRLAQRVPVRIRLDNQQ-GNLYPAGTTATVVIT 286
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
4-283 |
7.97e-71 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 221.46 E-value: 7.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 4 KTLKYFSTLFVLVLALIAGWWLWNFYMQS---PWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPY 80
Cdd:COG1566 2 KALKKRRLLALVLLLLALGLALWAAGRNGpdePVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 81 HIAVLNAQAQLA---------------------------KAQSDLAKANNEANRRRHL-SQNYISAEDLDTANLNVKAMQ 132
Cdd:COG1566 82 QAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALyKKGAVSQQELDEARAALDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 133 ASVNVAQ---------------------------ATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDS 185
Cdd:COG1566 162 AQLEAAQaqlaqaqaglreeeelaaaqaqvaqaeAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 186 HSFYVVGYFEETKLRHIREGSPAAITLYS-GSQTLQGHVSSIGRAIYDQSVetdsglvpdikPNVPWVRLAQRVPVRVEF 264
Cdd:COG1566 242 DDLWVEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTSP-----------PKNATGNVVQRYPVRIRL 310
|
330
....*....|....*....
gi 1278866364 265 DRlPEGITLVSGTTCTVSI 283
Cdd:COG1566 311 DN-PDPEPLRPGMSATVEI 328
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
32-235 |
3.32e-46 |
|
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: 157.59 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 32 SPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL 111
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 112 ----------------------------------------------SQNYISAEDLDTANLNVKAMQASVNV-------- 137
Cdd:pfam00529 88 eselaisrqdydgataqlraaqaavkaaqaqlaqaqidlarrrvlaPIGGISRESLVTAGALVAQAQANLLAtvaqldqi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 138 ----------------------------AQATLKQAQWELTQTVITAPVDGWVTNLSARV-GNYATTGQPVFALVDSHSF 188
Cdd:pfam00529 168 yvqitqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1278866364 189 YVVGYFEETKLRHIREGSPAAITLYSGSQTLQGHVSSIGRAIYDQSV 235
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-286 |
6.61e-43 |
|
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: 149.00 E-value: 6.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 38 GKVRAEQ-VSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL-SQNY 115
Cdd:TIGR01730 19 GSLEAVDeADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 116 ISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFE 195
Cdd:TIGR01730 99 VSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 196 ETKLRHIREGSPAAITLYS-GSQTLQGHVSSIgraiyDQSVETDSGLvpdikpnvpwvrlaqrVPVRVEFDRlPEGItLV 274
Cdd:TIGR01730 179 ERDLPQLRRGQTLTVELDAlPGEEFKGKLRFI-----DPRVDSGTGT----------------VRVRATFPN-PDGR-LL 235
|
250
....*....|..
gi 1278866364 275 SGTTCTVSIGSR 286
Cdd:TIGR01730 236 PGMFGRVTISLK 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
4-284 |
4.89e-76 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 234.25 E-value: 4.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 4 KTLKYFSTLFVLVLALIAGWWLWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIA 83
Cdd:PRK10559 7 KISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 84 VLNAQAQLAKAQSDLAKANNEANRRRHLSQNYISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVT 163
Cdd:PRK10559 87 LAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 164 NLSARVGNYATTGQPVFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGSQTLQGHVSSIGRAIYDQSVETDSGLVP 243
Cdd:PRK10559 167 NLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1278866364 244 DIKPNVPWVRLAQRVPVRVEFDRLPeGITLVSGTTCTVSIG 284
Cdd:PRK10559 247 TIDSNLEWVRLAQRVPVRIRLDNQQ-GNLYPAGTTATVVIT 286
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
4-283 |
7.97e-71 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 221.46 E-value: 7.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 4 KTLKYFSTLFVLVLALIAGWWLWNFYMQS---PWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPY 80
Cdd:COG1566 2 KALKKRRLLALVLLLLALGLALWAAGRNGpdePVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 81 HIAVLNAQAQLA---------------------------KAQSDLAKANNEANRRRHL-SQNYISAEDLDTANLNVKAMQ 132
Cdd:COG1566 82 QAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALyKKGAVSQQELDEARAALDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 133 ASVNVAQ---------------------------ATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDS 185
Cdd:COG1566 162 AQLEAAQaqlaqaqaglreeeelaaaqaqvaqaeAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 186 HSFYVVGYFEETKLRHIREGSPAAITLYS-GSQTLQGHVSSIGRAIYDQSVetdsglvpdikPNVPWVRLAQRVPVRVEF 264
Cdd:COG1566 242 DDLWVEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTSP-----------PKNATGNVVQRYPVRIRL 310
|
330
....*....|....*....
gi 1278866364 265 DRlPEGITLVSGTTCTVSI 283
Cdd:COG1566 311 DN-PDPEPLRPGMSATVEI 328
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
11-283 |
5.22e-57 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 186.39 E-value: 5.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 11 TLFVLVLALIAGWWLwnfyMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQ 90
Cdd:PRK10476 19 VALAIVALVFVIWRT----DSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 91 L-----------------------AKAQSDLAKANNE-ANRRRH-----LSQNYISAEDLDTANL--------------- 126
Cdd:PRK10476 95 LaladaqimttqrsvdaersnaasANEQVERARANAKlATRTLErleplLAKGYVSAQQVDQARTaqrdaevslnqallq 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 127 ---------NVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFEET 197
Cdd:PRK10476 175 aqaaaaavgGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 198 KLRHIREGSPAAITLYSGSQ-TLQGHVSSIGRAIYDqsveTDSGLVPDIKPNVP----WVRLAQRVPVRVEFDRLPEGIT 272
Cdd:PRK10476 255 DLKNIRVGDCATVYSMIDRGrPFEGKVDSIGWGVLP----DDGGNVPRGLPYVPrsinWVRVAQRFPVRIMLDKPDPELF 330
|
330
....*....|.
gi 1278866364 273 LVsGTTCTVSI 283
Cdd:PRK10476 331 RI-GASAVVEL 340
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
38-283 |
1.38e-53 |
|
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: 177.06 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 38 GKVRA-EQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHLS-QNY 115
Cdd:COG0845 16 GTVEArREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLkKGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 116 ISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFE 195
Cdd:COG0845 96 VSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 196 ETKLRHIREGSPAAITLYSGS-QTLQGHVSSIGRAIYDQSvetdsglvpdikpnvpwvrlaQRVPVRVEFDRlPEGiTLV 274
Cdd:COG0845 176 ESDLARLKVGQPVTVTLDAGPgKTFEGKVTFIDPAVDPAT---------------------RTVRVRAELPN-PDG-LLR 232
|
....*....
gi 1278866364 275 SGTTCTVSI 283
Cdd:COG0845 233 PGMFVRVRI 241
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
32-235 |
3.32e-46 |
|
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: 157.59 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 32 SPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL 111
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 112 ----------------------------------------------SQNYISAEDLDTANLNVKAMQASVNV-------- 137
Cdd:pfam00529 88 eselaisrqdydgataqlraaqaavkaaqaqlaqaqidlarrrvlaPIGGISRESLVTAGALVAQAQANLLAtvaqldqi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 138 ----------------------------AQATLKQAQWELTQTVITAPVDGWVTNLSARV-GNYATTGQPVFALVDSHSF 188
Cdd:pfam00529 168 yvqitqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1278866364 189 YVVGYFEETKLRHIREGSPAAITLYSGSQTLQGHVSSIGRAIYDQSV 235
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-286 |
6.61e-43 |
|
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: 149.00 E-value: 6.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 38 GKVRAEQ-VSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL-SQNY 115
Cdd:TIGR01730 19 GSLEAVDeADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 116 ISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFE 195
Cdd:TIGR01730 99 VSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 196 ETKLRHIREGSPAAITLYS-GSQTLQGHVSSIgraiyDQSVETDSGLvpdikpnvpwvrlaqrVPVRVEFDRlPEGItLV 274
Cdd:TIGR01730 179 ERDLPQLRRGQTLTVELDAlPGEEFKGKLRFI-----DPRVDSGTGT----------------VRVRATFPN-PDGR-LL 235
|
250
....*....|..
gi 1278866364 275 SGTTCTVSIGSR 286
Cdd:TIGR01730 236 PGMFGRVTISLK 247
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
12-265 |
4.82e-31 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 119.41 E-value: 4.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 12 LFVLV-LALIAGWWLWNFYMQSpwTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQ 90
Cdd:PRK15136 30 LFIIIgVAYGIYWFLVLRHHQE--TDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 91 LAKA---------------------QSDLAKANNEANRRRHL-SQNYISAEDLDTANLNVKAMQASVNVA---------- 138
Cdd:PRK15136 108 LANSvrqthqlminskqyqanielqKTALAQAQSDLNRRVPLgNANLIGREELQHARDAVASAQAQLDVAiqqynanqam 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 139 --------QATLKQAQWE-------LTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFEETKLRHIR 203
Cdd:PRK15136 188 ilntpledQPAVQQAATEvrnawlaLQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMR 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278866364 204 EGSPAAIT--LYSGSQTLQGHVSSIgraiyDQSVETDSGLVPDIKPNVPWVRLAQRVPVRVEFD 265
Cdd:PRK15136 268 IGQPATITsdIYGDDVVYTGKVVGL-----DMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELD 326
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
42-176 |
2.11e-22 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 95.63 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 42 AEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHLSQ-NYISAED 120
Cdd:PRK11556 85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKtNLVSRQE 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278866364 121 LDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTG 176
Cdd:PRK11556 165 LDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSG 220
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
4-216 |
3.44e-22 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 94.26 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 4 KTLKYFSTLFVLVLALIAGWWLWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIA 83
Cdd:PRK03598 3 KKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 84 VLNAQAQLAKAQSDLAK--------------------------ANNEANRRRHL-SQNYISAEDLDTANLN--------- 127
Cdd:PRK03598 83 LMQAKANVSVAQAQLDLmlagyrdeeiaqaraavkqaqaaydyAQNFYNRQQGLwKSRTISANDLENARSSrdqaqatlk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 128 -----------------VKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYV 190
Cdd:PRK03598 163 saqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWV 242
|
250 260
....*....|....*....|....*.
gi 1278866364 191 VGYFEETKLRHIREGSPaaITLYSGS 216
Cdd:PRK03598 243 RAYVDERNLGQAQPGRK--VLLYTDG 266
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
43-177 |
1.17e-16 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 78.99 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 43 EQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL-SQNYISAEDL 121
Cdd:PRK09859 60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLlKTNYVSRQDY 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278866364 122 DTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQ 177
Cdd:PRK09859 140 DTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQ 195
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
12-218 |
1.65e-14 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 72.88 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 12 LFVLVLALIAGWWLWNFYM----------------QSPWTRDGKVRA-EQVSITPQVSGSITTLLVKDNQYVKKGEELFR 74
Cdd:PRK11578 12 LIALVIVLAGGITLWRILNapvptyqtlivrpgdlQQSVLATGKLDAlRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 75 IDDTPYHIAV---------LNAQAQLAKAQSDLAKANneANRRRHLSQ-NYISAEDLDTA--NLNVKAMQ-----ASVNV 137
Cdd:PRK11578 92 IDPEQAENQIkeveatlmeLRAQRQQAEAELKLARVT--LSRQQRLAKtQAVSQQDLDTAatELAVKQAQigtidAQIKR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 138 AQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQP---VFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYS 214
Cdd:PRK11578 170 NQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLG 249
|
....
gi 1278866364 215 GSQT 218
Cdd:PRK11578 250 DPLT 253
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
38-265 |
2.37e-13 |
|
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: 67.53 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 38 GKVRAEQ---VSITPQVSGSITTLLVKDN-QYVKKGEELFRIDDTpyhiavlnaqaQLAKAQSDLAKANNEANRRRhlsq 113
Cdd:pfam16576 10 GRVAYDErrlAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSP-----------ELVAAQQEYLLALRSGDALS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 114 nyiSAEDLDTANLNVKAMQasvnVAQATLkqAQWELTQTV-----ITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSF 188
Cdd:pfam16576 75 ---KSELLRAARQRLRLLG----MPEAQI--AELERTGKVqptvtVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278866364 189 YVVGYFEETKLRHIREGSPAAITL-YSGSQTLQGHVSSIGraiydqsvetdsglvPDIKPNvpwvrlAQRVPVRVEFD 265
Cdd:pfam16576 146 WVEADVPEQDLALVKVGQPAEVTLpALPGKTFEGKVDYIY---------------PTLDPK------TRTVRVRIELP 202
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
43-92 |
4.24e-13 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 62.46 E-value: 4.24e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1278866364 43 EQVSITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLA 92
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
36-160 |
1.36e-12 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 67.13 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 36 RDGKVRAeqvsitpQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANRRRHL-SQN 114
Cdd:PRK09578 62 RQAEVRA-------RVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLvRDR 134
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1278866364 115 YISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDG 160
Cdd:PRK09578 135 AVSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDG 180
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
38-177 |
1.57e-12 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 67.05 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 38 GKVRAEQVS-ITPQVSGSITTLLVKDNQYVKKGEELFRIDDTPYHIAVLNAQAQLAKAQSDLAKANNEANR-RRHLSQNY 115
Cdd:PRK15030 58 GRTSAYRIAeVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRyQKLLGTQY 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278866364 116 ISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQTVITAPVDGWVTNLSARVGNYATTGQ 177
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQ 199
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
153-276 |
1.44e-09 |
|
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: 54.29 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 153 VITAPVDGWVTNLSARVGNYATTGQPVFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGS-QTLQGHVSSIGRAIY 231
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSdYTLEGKVVRISPTVD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1278866364 232 DQSvetdsglvpdikpnvpwvrlaQRVPVRVEFDRLPEGITLVSG 276
Cdd:pfam13437 81 PDT---------------------GVIPVRVSIENPKTPIPLLPG 104
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
83-151 |
4.68e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.33 E-value: 4.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 83 AVLNAQAQLAKAQSDLAKANNE-ANRRRHLSQnyISAEDLDTANLNVKAMQASVNVAQATLKQAQWELTQ 151
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAAAQAAlATAQKELAN--AQAQALQTAQNNLATAQAALANAEARLAKAKEALAN 343
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
84-174 |
2.85e-03 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 38.89 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866364 84 VLNAQAQLAKAQSDLAKANN----------------------EANRRRHLSQNYISAEDLDTA-NLNVKAMQASVNVAQA 140
Cdd:TIGR01844 160 VLQAEARYASARAQLIQAQNnlddakaqlrrlvgqpelaplaVPSFPAELPEPLDQLLEIAEAsNPLLLAAQAAVDAARY 239
|
90 100 110
....*....|....*....|....*....|....
gi 1278866364 141 TLKQAQWELTQTVitapvdgwvtNLSARVGNYAT 174
Cdd:TIGR01844 240 QVEQARAGHLPTL----------SLTASTGNSDT 263
|
|
| |
