|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
26-284 |
2.17e-73 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 227.32 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 26 WNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEA 105
Cdd:PRK10559 29 WVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 106 NRRRHLSQNYISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDS 185
Cdd:PRK10559 109 GRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 186 HSFYVVGYFEETKLRHIREGSPAAITLYSGSQKLQGHVSSIGRAIYDQSVETDSGLVPDIKPNVPWVRLAQRVPVRVEFD 265
Cdd:PRK10559 189 NSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIRLD 268
|
250
....*....|....*....
gi 658547289 266 RLPQDItLVSGTTCTVSIG 284
Cdd:PRK10559 269 NQQGNL-YPAGTTATVVIT 286
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
23-283 |
1.74e-68 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 215.68 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 23 WWMWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLA---------- 92
Cdd:COG1566 24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarle 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 93 -----------------KAQSDLAKANNEANRRRHL-SQNYISAEDLDTANINVKAMQAN-------------------- 134
Cdd:COG1566 104 aelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALyKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeee 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 135 -------VNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGSP 207
Cdd:COG1566 184 laaaqaqVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547289 208 AAITLYS-GSQKLQGHVSSIGRAIYDQSVetdsglvpdikPNVPWVRLAQRVPVRVEFDRlPQDITLVSGTTCTVSI 283
Cdd:COG1566 264 VEVRVDAyPDRVFEGKVTSISPGAGFTSP-----------PKNATGNVVQRYPVRIRLDN-PDPEPLRPGMSATVEI 328
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
32-235 |
8.59e-47 |
|
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: 159.13 E-value: 8.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 32 SPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL 111
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 112 ----------------------------------------------SQNYISAEDLDTANINVKAMQANVNV-------- 137
Cdd:pfam00529 88 eselaisrqdydgataqlraaqaavkaaqaqlaqaqidlarrrvlaPIGGISRESLVTAGALVAQAQANLLAtvaqldqi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 138 ----------------------------AEATLKQAQWQLTQTVITAPVDGWVTNLSARV-GNYATTGQPIFALVDSHSF 188
Cdd:pfam00529 168 yvqitqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658547289 189 YVVGYFEETKLRHIREGSPAAITLYSGSQKLQGHVSSIGRAIYDQSV 235
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-283 |
1.29e-42 |
|
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: 148.23 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRAEQ-VSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL-SQNY 115
Cdd:TIGR01730 19 GSLEAVDeADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 116 ISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFE 195
Cdd:TIGR01730 99 VSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 196 ETKLRHIREGSPAAITLYS-GSQKLQGHVSSIgraiyDQSVETDSGLvpdikpnvpwvrlaqrVPVRVEFDRLPQdiTLV 274
Cdd:TIGR01730 179 ERDLPQLRRGQTLTVELDAlPGEEFKGKLRFI-----DPRVDSGTGT----------------VRVRATFPNPDG--RLL 235
|
....*....
gi 658547289 275 SGTTCTVSI 283
Cdd:TIGR01730 236 PGMFGRVTI 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
26-284 |
2.17e-73 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 227.32 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 26 WNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEA 105
Cdd:PRK10559 29 WVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 106 NRRRHLSQNYISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDS 185
Cdd:PRK10559 109 GRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 186 HSFYVVGYFEETKLRHIREGSPAAITLYSGSQKLQGHVSSIGRAIYDQSVETDSGLVPDIKPNVPWVRLAQRVPVRVEFD 265
Cdd:PRK10559 189 NSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIRLD 268
|
250
....*....|....*....
gi 658547289 266 RLPQDItLVSGTTCTVSIG 284
Cdd:PRK10559 269 NQQGNL-YPAGTTATVVIT 286
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
23-283 |
1.74e-68 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 215.68 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 23 WWMWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLA---------- 92
Cdd:COG1566 24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarle 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 93 -----------------KAQSDLAKANNEANRRRHL-SQNYISAEDLDTANINVKAMQAN-------------------- 134
Cdd:COG1566 104 aelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALyKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeee 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 135 -------VNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGSP 207
Cdd:COG1566 184 laaaqaqVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547289 208 AAITLYS-GSQKLQGHVSSIGRAIYDQSVetdsglvpdikPNVPWVRLAQRVPVRVEFDRlPQDITLVSGTTCTVSI 283
Cdd:COG1566 264 VEVRVDAyPDRVFEGKVTSISPGAGFTSP-----------PKNATGNVVQRYPVRIRLDN-PDPEPLRPGMSATVEI 328
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
31-283 |
3.33e-57 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 186.77 E-value: 3.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 31 QSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQL------------------- 91
Cdd:PRK10476 35 SAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLaladaqimttqrsvdaers 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 92 ----AKAQSDLAKANNE-ANRRRH-----LSQNYISAEDLDTANI------------------------NVKAMQANVNV 137
Cdd:PRK10476 115 naasANEQVERARANAKlATRTLErleplLAKGYVSAQQVDQARTaqrdaevslnqallqaqaaaaavgGVDALVAQRAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 138 AEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGSQ 217
Cdd:PRK10476 195 REAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRG 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658547289 218 K-LQGHVSSIGRAIYDqsveTDSGLVPDIKPNVP----WVRLAQRVPVRVEFDRLPQDITLVsGTTCTVSI 283
Cdd:PRK10476 275 RpFEGKVDSIGWGVLP----DDGGNVPRGLPYVPrsinWVRVAQRFPVRIMLDKPDPELFRI-GASAVVEL 340
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
38-283 |
1.42e-55 |
|
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: 182.07 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRA-EQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHLS-QNY 115
Cdd:COG0845 16 GTVEArREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLkKGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 116 ISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFE 195
Cdd:COG0845 96 VSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 196 ETKLRHIREGSPAAITLYSGSQK-LQGHVSSIGRAIYDQSvetdsglvpdikpnvpwvrlaQRVPVRVEFDrlPQDITLV 274
Cdd:COG0845 176 ESDLARLKVGQPVTVTLDAGPGKtFEGKVTFIDPAVDPAT---------------------RTVRVRAELP--NPDGLLR 232
|
....*....
gi 658547289 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 |
8.59e-47 |
|
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: 159.13 E-value: 8.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 32 SPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL 111
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 112 ----------------------------------------------SQNYISAEDLDTANINVKAMQANVNV-------- 137
Cdd:pfam00529 88 eselaisrqdydgataqlraaqaavkaaqaqlaqaqidlarrrvlaPIGGISRESLVTAGALVAQAQANLLAtvaqldqi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 138 ----------------------------AEATLKQAQWQLTQTVITAPVDGWVTNLSARV-GNYATTGQPIFALVDSHSF 188
Cdd:pfam00529 168 yvqitqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658547289 189 YVVGYFEETKLRHIREGSPAAITLYSGSQKLQGHVSSIGRAIYDQSV 235
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-283 |
1.29e-42 |
|
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: 148.23 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRAEQ-VSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL-SQNY 115
Cdd:TIGR01730 19 GSLEAVDeADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 116 ISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFE 195
Cdd:TIGR01730 99 VSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 196 ETKLRHIREGSPAAITLYS-GSQKLQGHVSSIgraiyDQSVETDSGLvpdikpnvpwvrlaqrVPVRVEFDRLPQdiTLV 274
Cdd:TIGR01730 179 ERDLPQLRRGQTLTVELDAlPGEEFKGKLRFI-----DPRVDSGTGT----------------VRVRATFPNPDG--RLL 235
|
....*....
gi 658547289 275 SGTTCTVSI 283
Cdd:TIGR01730 236 PGMFGRVTI 244
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
35-265 |
8.55e-31 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 118.64 E-value: 8.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 35 TRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDT------------------PYHIAILNA---QAQLAK 93
Cdd:PRK15136 52 TDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTdaeqafekaktalansvrQTHQLMINSkqyQANIEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 94 AQSDLAKANNEANRRRHL-SQNYISAEDLDTANINVKAMQANVNVA------------------EATLKQAQWQ------ 148
Cdd:PRK15136 132 QKTALAQAQSDLNRRVPLgNANLIGREELQHARDAVASAQAQLDVAiqqynanqamilntpledQPAVQQAATEvrnawl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 149 -LTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGSPAAIT--LYSGSQKLQGHVSS 225
Cdd:PRK15136 212 aLQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITsdIYGDDVVYTGKVVG 291
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 658547289 226 IgraiyDQSVETDSGLVPDIKPNVPWVRLAQRVPVRVEFD 265
Cdd:PRK15136 292 L-----DMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELD 326
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
42-191 |
4.26e-24 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 100.63 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 42 AEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHLSQ-NYISAED 120
Cdd:PRK11556 85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKtNLVSRQE 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547289 121 LDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQ--PIFALVDSHSFYVV 191
Cdd:PRK11556 165 LDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDttGIVVITQTHPIDLV 237
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
20-237 |
5.18e-19 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 85.40 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 20 VAGWWMWNFYMQSPWTRDGKVRAEQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLA 99
Cdd:PRK03598 19 AGGWWWYQSRQDNGLTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 100 K--------------------------ANNEANRRRHL-SQNYISAEDLDTANIN------------------------- 127
Cdd:PRK03598 99 LmlagyrdeeiaqaraavkqaqaaydyAQNFYNRQQGLwKSRTISANDLENARSSrdqaqatlksaqdklsqyregnrpq 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 128 -VKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGS 206
Cdd:PRK03598 179 dIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGR 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 658547289 207 PaaITLYSGSQKLQGHVSSIG----RAIYD-QSVET 237
Cdd:PRK03598 259 K--VLLYTDGRPDKPYHGQIGfvspTAEFTpKTVET 292
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
43-177 |
1.08e-17 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 82.07 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 43 EQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL-SQNYISAEDL 121
Cdd:PRK09859 60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLlKTNYVSRQDY 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 658547289 122 DTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQ 177
Cdd:PRK09859 140 DTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQ 195
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
43-92 |
4.66e-15 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 67.85 E-value: 4.66e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658547289 43 EQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLA 92
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
36-160 |
1.45e-13 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 70.21 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 36 RDGKVRAeqvsitpQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANRRRHL-SQN 114
Cdd:PRK09578 62 RQAEVRA-------RVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLvRDR 134
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 658547289 115 YISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDG 160
Cdd:PRK09578 135 AVSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDG 180
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
38-218 |
1.47e-13 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 69.80 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRA-EQVSITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAI---------LNAQAQLAKAQSDLAKANneANR 107
Cdd:PRK11578 54 GKLDAlRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIkeveatlmeLRAQRQQAEAELKLARVT--LSR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 108 RRHLSQ-NYISAEDLDTA-------NINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQP- 178
Cdd:PRK11578 132 QQRLAKtQAVSQQDLDTAatelavkQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQa 211
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658547289 179 --IFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGSQK 218
Cdd:PRK11578 212 pnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLT 253
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
38-265 |
3.85e-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: 66.76 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRAEQ---VSITPQVSGSITTLLVKDN-QFVKKGDILFRIddtpYHIAILNAQAQLAKAQSdlakanneanrrrhlSQ 113
Cdd:pfam16576 10 GRVAYDErrlAHVHARVEGWIEKLYVNATgDPVKKGQPLAEL----YSPELVAAQQEYLLALR---------------SG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 114 NYISAEDLdtaninVKAMQA---NVNVAEATLKQ--AQWQLTQTV-ITAPVDGWVTNLSARVGNYATTGQPIFALVDSHS 187
Cdd:pfam16576 71 DALSKSEL------LRAARQrlrLLGMPEAQIAEleRTGKVQPTVtVYAPISGVVTELNVREGMYVQPGDTLFTIADLST 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547289 188 FYVVGYFEETKLRHIREGSPAAITL-YSGSQKLQGHVSSIGraiydqsvetdsglvPDIKPNvpwvrlAQRVPVRVEFD 265
Cdd:pfam16576 145 VWVEADVPEQDLALVKVGQPAEVTLpALPGKTFEGKVDYIY---------------PTLDPK------TRTVRVRIELP 202
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
38-177 |
1.47e-11 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 63.96 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 38 GKVRAEQVS-ITPQVSGSITTLLVKDNQFVKKGDILFRIDDTPYHIAILNAQAQLAKAQSDLAKANNEANR-RRHLSQNY 115
Cdd:PRK15030 58 GRTSAYRIAeVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRyQKLLGTQY 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658547289 116 ISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQTVITAPVDGWVTNLSARVGNYATTGQ 177
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQ 199
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
153-276 |
2.40e-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: 53.91 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 153 VITAPVDGWVTNLSARVGNYATTGQPIFALVDSHSFYVVGYFEETKLRHIREGSPAAITLYSGS-QKLQGHVSSIGRAIY 231
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSdYTLEGKVVRISPTVD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 658547289 232 DQSvetdsglvpdikpnvpwvrlaQRVPVRVEFDRLPQDITLVSG 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 |
6.96e-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: 43.56 E-value: 6.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 83 AILNAQAQLAKAQSDLAKANNE-ANRRRHLSQnyISAEDLDTANINVKAMQANVNVAEATLKQAQWQLTQ 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 |
3.86e-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: 38.51 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547289 84 ILNAQAQLAKAQSDLAKANN----------------------EANRRRHLSQNYISAEDLDTANI-NVKAMQANVNVAEA 140
Cdd:TIGR01844 160 VLQAEARYASARAQLIQAQNnlddakaqlrrlvgqpelaplaVPSFPAELPEPLDQLLEIAEASNpLLLAAQAAVDAARY 239
|
90 100 110
....*....|....*....|....*....|....
gi 658547289 141 TLKQAQWQLTQTVitapvdgwvtNLSARVGNYAT 174
Cdd:TIGR01844 240 QVEQARAGHLPTL----------SLTASTGNSDT 263
|
|
| |
