|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-367 |
4.62e-83 |
|
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: 257.18 E-value: 4.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 42 KVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSD 121
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 122 NEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADvTALT 201
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 202 SVVSTDKVYAYFDADERVFLKYtelarqgRRGAttPVYLGLSNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEY 281
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARL-------KVGQ--PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 282 TPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEGD-KPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQRVR 360
Cdd:COG0845 232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311
|
....*..
gi 1509074363 361 PGSPVAP 367
Cdd:COG0845 312 DGAKVRV 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-365 |
6.91e-68 |
|
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: 217.95 E-value: 6.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 38 VSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAA 117
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 118 TRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADV 197
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 198 TALTsVVSTDKVYAYFDADERVFLKYtelarqgRRGATTPVylGLSNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNS 277
Cdd:TIGR01730 161 TLAT-IVDLDPLEADFSVPERDLPQL-------RRGQTLTV--ELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 278 KGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEGD-KPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGL 356
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGV 310
|
....*....
gi 1509074363 357 QRVRPGSPV 365
Cdd:TIGR01730 311 VKLRDGAKV 319
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
45-353 |
1.50e-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: 165.29 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 45 EQPVNEWDEFTGRLEA-PETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNE 123
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 124 AQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVT-ADVTALTS 202
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAqAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 203 VVSTDKVYAYFDADERVFLKYTELARQGRRG--ATTPVYLGLSNETG------NPHLGQMNFVDNQVNPATGTIRGRAVF 274
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLqiAEAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 275 DN-SKGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEG--DKPAYRSVELGPKIEGLRIVRSGLNKEDTI 351
Cdd:pfam00529 241 VVpEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGisPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 1509074363 352 IV 353
Cdd:pfam00529 321 RL 322
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
8-362 |
2.90e-46 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 163.35 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 8 LRFPLaILAVVVMSACGKTPEQAAAMPAAKVSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKK 87
Cdd:PRK09859 7 LLIPL-LFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 88 GDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKL 167
Cdd:PRK09859 86 GDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 168 NLSFTRVTSPISGRVSRAEITAGNLVTADVT-ALTSVVSTDKVYAYFDADERVFLKYTELARQG---RRGATTPVYLGLS 243
Cdd:PRK09859 166 NLQYANVTSPITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGqikQVQGSTPVQLNLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 244 NETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDL-GKKFVLVMEGD 322
Cdd:PRK09859 246 NGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAqGKATALILDKD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1509074363 323 KPA-YRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQRVRPG 362
Cdd:PRK09859 326 DVVqLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-367 |
4.62e-83 |
|
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: 257.18 E-value: 4.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 42 KVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSD 121
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 122 NEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADvTALT 201
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 202 SVVSTDKVYAYFDADERVFLKYtelarqgRRGAttPVYLGLSNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEY 281
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARL-------KVGQ--PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 282 TPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEGD-KPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQRVR 360
Cdd:COG0845 232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311
|
....*..
gi 1509074363 361 PGSPVAP 367
Cdd:COG0845 312 DGAKVRV 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-365 |
6.91e-68 |
|
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: 217.95 E-value: 6.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 38 VSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAA 117
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 118 TRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADV 197
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 198 TALTsVVSTDKVYAYFDADERVFLKYtelarqgRRGATTPVylGLSNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNS 277
Cdd:TIGR01730 161 TLAT-IVDLDPLEADFSVPERDLPQL-------RRGQTLTV--ELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 278 KGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEGD-KPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGL 356
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGV 310
|
....*....
gi 1509074363 357 QRVRPGSPV 365
Cdd:TIGR01730 311 VKLRDGAKV 319
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
45-353 |
1.50e-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: 165.29 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 45 EQPVNEWDEFTGRLEA-PETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNE 123
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 124 AQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVT-ADVTALTS 202
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAqAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 203 VVSTDKVYAYFDADERVFLKYTELARQGRRG--ATTPVYLGLSNETG------NPHLGQMNFVDNQVNPATGTIRGRAVF 274
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLqiAEAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 275 DN-SKGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMEG--DKPAYRSVELGPKIEGLRIVRSGLNKEDTI 351
Cdd:pfam00529 241 VVpEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGisPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 1509074363 352 IV 353
Cdd:pfam00529 321 RL 322
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
8-362 |
2.90e-46 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 163.35 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 8 LRFPLaILAVVVMSACGKTPEQAAAMPAAKVSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKK 87
Cdd:PRK09859 7 LLIPL-LFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 88 GDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKL 167
Cdd:PRK09859 86 GDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 168 NLSFTRVTSPISGRVSRAEITAGNLVTADVT-ALTSVVSTDKVYAYFDADERVFLKYTELARQG---RRGATTPVYLGLS 243
Cdd:PRK09859 166 NLQYANVTSPITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGqikQVQGSTPVQLNLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 244 NETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDL-GKKFVLVMEGD 322
Cdd:PRK09859 246 NGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAqGKATALILDKD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1509074363 323 KPA-YRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQRVRPG 362
Cdd:PRK09859 326 DVVqLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
11-387 |
2.51e-43 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 156.03 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 11 PLAILAVV----VMSACGKTPEQAAAMPAAKVSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVK 86
Cdd:PRK15030 9 PLAVVLMLsgslALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 87 KGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAK 166
Cdd:PRK15030 89 AGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 167 LNLSFTRVTSPISGRVSRAEITAGNLV-TADVTALTSVVSTDKVYAYFDADERVFLKYTELARQG---RRGATTPVYLGL 242
Cdd:PRK15030 169 INLAYTKVTSPISGRIGKSNVTEGALVqNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGtlkQENGKAKVSLIT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 243 SNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEYTPGLYARLKLVGSGTYSAVLINDEAVG-TDLGKKFVLVMEG 321
Cdd:PRK15030 249 SDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVVGA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509074363 322 D-KPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQRVRPGSPVAPETIPMASKETLAALAQQRQA 387
Cdd:PRK15030 329 DdKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQS 395
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
1-391 |
4.74e-38 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 141.47 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 1 MEQSLKHLRFPLAILAVVVMSACGKTPEQAAAMPAAKVSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFT 80
Cdd:PRK09578 1 YEWARRRRLLLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 81 EGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQA 160
Cdd:PRK09578 81 EGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 161 QLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTAD-VTALTSVVSTDKVYAYFD---ADERVFLKYTELAR-QGRRGAT 235
Cdd:PRK09578 161 ELARAQLQLDYATVTAPIDGRARRALVTEGALVGQDqATPLTTVEQLDPIYVNFSqpaADVEALRRAVKSGRaTGIAQQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 236 TPVYLGLSNETGNPHLGQMNFVDNQVNPATGTIRGRAVFDNSKGEYTPGLYARLKLVGSGTYSAVLINDEAvgtdlgkkf 315
Cdd:PRK09578 241 VAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDA--------- 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509074363 316 vLVMEGDKPAYRSVELGPKIEGLRIVRSGLNKEDTIIVKGLQrvrPGSPVAPETIP-MASKETLAALAQQRQALEAS 391
Cdd:PRK09578 312 -LLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLA---GGERVIVDNAAqFAPGTAVKAVERAPAAKPAP 384
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
32-386 |
5.39e-35 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 133.76 E-value: 5.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 32 AMPAAKVSVAKVLEQPVNEWDEFTGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQ 111
Cdd:PRK11556 56 SGPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 112 QTRAAATRSDNEAQRGERLRQSNAISAELADSRTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGN 191
Cdd:PRK11556 136 KDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 192 LVTA-DVTALTSVVSTDKVYAYFDADERvflKYTELARQGRRGATTPVYLGLSNETGNPHLGQMNFVDNQVNPATGTIRG 270
Cdd:PRK11556 216 QISSgDTTGIVVITQTHPIDLVFTLPES---DIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 271 RAVFDNSKGEYTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVM-EGDKPAYRSVELGPKIEGLRIVRSGLNKED 349
Cdd:PRK11556 293 KARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLnDENKVSKHLVTPGIQDSQKVVISAGLSAGD 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 1509074363 350 TIIVKGLQRVRPGSPVapETIPMASKETLAALAQQRQ 386
Cdd:PRK11556 373 RVVTDGIDRLTEGAKV--EVVEPQSATTPEEKATSRE 407
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
55-222 |
9.53e-22 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 95.11 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 55 TGRLEApETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSD------------- 121
Cdd:COG1566 38 DGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiaaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 122 --------------NEAQRGERLRQSNAISA-ELADSRT--------------------------TAAQEARAAVAGIQA 160
Cdd:COG1566 117 aqlaaaqaqldlaqRELERYQALYKKGAVSQqELDEARAaldaaqaqleaaqaqlaqaqaglreeEELAAAQAQVAQAEA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1509074363 161 QLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADvTALTSVVSTDKVY--AYFDADERVFLK 222
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAG-QPLLTIVPLDDLWveAYVPETDLGRVK 259
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
55-195 |
4.43e-15 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 75.97 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 55 TGRLEAPETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEA-------QRG 127
Cdd:PRK11578 53 TGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELklarvtlSRQ 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1509074363 128 ERLRQSNAISAELADSRTTAAQEARAAVAGIQAQ-------LDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTA 195
Cdd:PRK11578 133 QRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQikrnqasLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIA 207
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
64-237 |
5.05e-14 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 72.47 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 64 VQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAAATRSDNEAQRGERLRQSnAISAELADS 143
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQ-AMSREEIDQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 144 RTTAAQEARAAVAGIQAQLDLAKLNLSFTRVTSPISGRVSRAEITAGNLVTADVTALtSVVSTDKVY--AYfdadervfL 221
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAV-ALVKQNSFYvlAY--------M 197
|
170
....*....|....*...
gi 1509074363 222 KYTELA--RQGRRGATTP 237
Cdd:PRK10559 198 EETKLEgvRPGYRAEITP 215
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
62-211 |
1.22e-12 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 68.51 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 62 ETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQQTRAA------------------------- 116
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQimttqrsvdaersnaasaneqvera 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 117 ------ATRSdneAQRGERLRQSNAISAE-LADSRT-----------------------TAAQEARAAVAGIQAQLDLAK 166
Cdd:PRK10476 127 ranaklATRT---LERLEPLLAKGYVSAQqVDQARTaqrdaevslnqallqaqaaaaavGGVDALVAQRAAREAALAIAE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1509074363 167 LNLSFTRVTSPISGRVSRAEITAGNLVTADVTALTsVVSTDKVYA 211
Cdd:PRK10476 204 LHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFT-LIDTDHWYA 247
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
62-111 |
3.46e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 57.84 E-value: 3.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1509074363 62 ETVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQAEVRRLEAQLQ 111
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
63-214 |
5.90e-10 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 60.36 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 63 TVQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPF-------QAEVRRLEAQLQ-------------------QTRAA 116
Cdd:PRK03598 43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYenalmqaKANVSVAQAQLDlmlagyrdeeiaqaraavkQAQAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 117 ATRSDNEAQRGERLRQSNAISA-ELADSRTTAAQEARAAVAGI-------------------------QAQLDLAKLNLS 170
Cdd:PRK03598 123 YDYAQNFYNRQQGLWKSRTISAnDLENARSSRDQAQATLKSAQdklsqyregnrpqdiaqakaslaqaQAALAQAELNLQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1509074363 171 FTRVTSPISGRV-SRAeITAGNLVTADVTALTsvVSTDK---VYAYFD 214
Cdd:PRK03598 203 DTELIAPSDGTIlTRA-VEPGTMLNAGSTVFT--LSLTRpvwVRAYVD 247
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
55-287 |
8.64e-10 |
|
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: 58.29 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 55 TGRLEAPET--VQIRPRVSGQIDQV-AFTEGALVKKGDLLFQID-PRPFQAEVRRLEAqLQQTRAAATRSDNEAQRgERL 130
Cdd:pfam16576 9 VGRVAYDERrlAHVHARVEGWIEKLyVNATGDPVKKGQPLAELYsPELVAAQQEYLLA-LRSGDALSKSELLRAAR-QRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 131 RQ---SNAISAELADSRTTAAqearaavagiqaqldlaklnlSFTrVTSPISGRVSRAEITAGNLVTADvTALTSVVSTD 207
Cdd:pfam16576 87 RLlgmPEAQIAELERTGKVQP---------------------TVT-VYAPISGVVTELNVREGMYVQPG-DTLFTIADLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 208 KVYAYFDADERvflkytELARQgRRGATTPVYL-GLSNETGNphlGQMNFVDNQVNPATGTIRGRAVFDNSKGEYTPGLY 286
Cdd:pfam16576 144 TVWVEADVPEQ------DLALV-KVGQPAEVTLpALPGKTFE---GKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMF 213
|
.
gi 1509074363 287 A 287
Cdd:pfam16576 214 A 214
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
64-227 |
1.97e-05 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 46.61 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 64 VQIRPRVSGQIDQVAFTEGALVKKGDLLFQIDPRPFQ---------------------AEVRRLEAQLQQTRAAATRSDN 122
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEqafekaktalansvrqthqlmINSKQYQANIELQKTALAQAQS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509074363 123 EAQRGERLRQSNAISAE-LADSRTTAAQEARAAVAGIQ------------------------AQLDLAKLNLSFTRVTSP 177
Cdd:PRK15136 142 DLNRRVPLGNANLIGREeLQHARDAVASAQAQLDVAIQqynanqamilntpledqpavqqaaTEVRNAWLALQRTKIVSP 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1509074363 178 ISGRVSRAEITAGNLVTADvTALTSVVSTDKVYAyfDADervfLKYTELA 227
Cdd:PRK15136 222 MTGYVSRRSVQVGAQISPT-TPLMAVVPATNLWV--DAN----FKETQLA 264
|
|
| |
