|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
36-346 |
6.18e-77 |
|
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: 242.54 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 36 KAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSLALAK 108
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaalaQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 109 SKLKRVQELLKKQpdSMSQQDVEELGE-----QANLAAA--DFRQKEALMNDYLLVAPFDGQLTNFTHSVGSKIDSATAL 181
Cdd:COG0845 82 AELERYKALLKKG--AVSQQELDQAKAaldqaQAALAAAqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 182 VSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFAKV 261
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 262 SQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVnTNDGYVVVEKGLKLGDNVVVTGQQNLKKASLVKV 340
Cdd:COG0845 240 RIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGR-RDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRV 318
|
....*.
gi 857909417 341 MNPNAE 346
Cdd:COG0845 319 VEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
32-340 |
4.41e-59 |
|
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: 196.38 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 32 VTIEKAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSL 104
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDdyqlalqAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 105 ALAKSKLKRVQELLKKQPDSM-----SQQDVEELGEQANLAAADFRQKEALMNDYLLVAPFDGQLTNFTHSVGSKIDSAT 179
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQadlddAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 180 ALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFA 259
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 260 KVSQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVnTNDGYVVVEKGLKLGDNVVVTGQQNLKKASLV 338
Cdd:TIGR01730 241 RVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGL-RNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319
|
..
gi 857909417 339 KV 340
Cdd:TIGR01730 320 KV 321
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
27-367 |
4.09e-23 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 100.63 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 27 SNLIPVTIEKAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDN-------TKAKADLDK 99
Cdd:PRK11556 57 GPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPrpfkvalAQAQGQLAK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 100 ARSSLALAKSKLKRVQELLKKQpdSMSQQdveELGEQANLAaadfRQKEA-------------LMNDY-LLVAPFDGQLT 165
Cdd:PRK11556 137 DQATLANARRDLARYQQLAKTN--LVSRQ---ELDAQQALV----SETEGtikadeasvasaqLQLDYsRITAPISGRVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 166 NFTHSVGSKIDS--ATALVSLIKLDPVEVQYSIGQSDLGNA----KLGQNVSiqVDAFvDEAFS-----GVVDYIAPAVD 234
Cdd:PRK11556 208 LKQVDVGNQISSgdTTGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLV--VEAW-DRTNSkklseGTLLSLDNQID 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 235 ESSGRVEVHAHVTNPEHRLVPGMFAKVSQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVNtNDGYVV 313
Cdd:PRK11556 285 ATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDEnKVSKHLVTPGIQ-DSQKVV 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 857909417 314 VEKGLKLGDNVVVTGQQNLKKASLVKVMNPNAEQKTVelitEPTSKENTQQTAE 367
Cdd:PRK11556 364 ISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE----EKATSREYAKKGA 413
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
76-259 |
1.07e-19 |
|
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: 87.18 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 76 GDSVKKGELI----------AQLDNTKAKADLDKARSS--LALAKSKLKrvqeLLKkqpdsMSQQDVEELGeqanlaaad 143
Cdd:pfam16576 39 GDPVKKGQPLaelyspelvaAQQEYLLALRSGDALSKSelLRAARQRLR----LLG-----MPEAQIAELE--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 144 fRQKEALMNdYLLVAPFDGQLTNFTHSVGSKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFS 223
Cdd:pfam16576 101 -RTGKVQPT-VTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFE 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 857909417 224 GVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFA 259
Cdd:pfam16576 179 GKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
36-346 |
6.18e-77 |
|
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: 242.54 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 36 KAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSLALAK 108
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaalaQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 109 SKLKRVQELLKKQpdSMSQQDVEELGE-----QANLAAA--DFRQKEALMNDYLLVAPFDGQLTNFTHSVGSKIDSATAL 181
Cdd:COG0845 82 AELERYKALLKKG--AVSQQELDQAKAaldqaQAALAAAqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 182 VSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFAKV 261
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 262 SQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVnTNDGYVVVEKGLKLGDNVVVTGQQNLKKASLVKV 340
Cdd:COG0845 240 RIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGR-RDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRV 318
|
....*.
gi 857909417 341 MNPNAE 346
Cdd:COG0845 319 VEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
32-340 |
4.41e-59 |
|
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: 196.38 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 32 VTIEKAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSL 104
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDdyqlalqAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 105 ALAKSKLKRVQELLKKQPDSM-----SQQDVEELGEQANLAAADFRQKEALMNDYLLVAPFDGQLTNFTHSVGSKIDSAT 179
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQadlddAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 180 ALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFA 259
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 260 KVSQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVnTNDGYVVVEKGLKLGDNVVVTGQQNLKKASLV 338
Cdd:TIGR01730 241 RVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGL-RNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319
|
..
gi 857909417 339 KV 340
Cdd:TIGR01730 320 KV 321
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-261 |
6.66e-31 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 121.31 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 1 MKFTKLSKTICLALFALhispsfaqdsnLIPVTIEKAHKQAFTSSINEVGKIRAtDSAALTFSASDKILNIHFKDGDSVK 80
Cdd:COG1566 1 MKALKKRRLLALVLLLL-----------ALGLALWAAGRNGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 81 KGELIAQLDNT----------------------------------KAKADLDKARSSLALAKSKLKRVQELLKKQpdSMS 126
Cdd:COG1566 69 KGQVLARLDPTdlqaalaqaeaqlaaaeaqlarleaelgaeaeiaAAEAQLAAAQAQLDLAQRELERYQALYKKG--AVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 127 QQDVEE-------------------------LGEQANL---------AAADFRQKEALMNDYLLVAPFDGQLTNFTHSVG 172
Cdd:COG1566 147 QQELDEaraaldaaqaqleaaqaqlaqaqagLREEEELaaaqaqvaqAEAALAQAELNLARTTIRAPVDGVVTNLNVEPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 173 SKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSG----------RVEV 242
Cdd:COG1566 227 EVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPpknatgnvvqRYPV 306
|
330 340
....*....|....*....|
gi 857909417 243 HAHVTNPE-HRLVPGMFAKV 261
Cdd:COG1566 307 RIRLDNPDpEPLRPGMSATV 326
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
27-367 |
4.09e-23 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 100.63 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 27 SNLIPVTIEKAHKQAFTSSINEVGKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDN-------TKAKADLDK 99
Cdd:PRK11556 57 GPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPrpfkvalAQAQGQLAK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 100 ARSSLALAKSKLKRVQELLKKQpdSMSQQdveELGEQANLAaadfRQKEA-------------LMNDY-LLVAPFDGQLT 165
Cdd:PRK11556 137 DQATLANARRDLARYQQLAKTN--LVSRQ---ELDAQQALV----SETEGtikadeasvasaqLQLDYsRITAPISGRVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 166 NFTHSVGSKIDS--ATALVSLIKLDPVEVQYSIGQSDLGNA----KLGQNVSiqVDAFvDEAFS-----GVVDYIAPAVD 234
Cdd:PRK11556 208 LKQVDVGNQISSgdTTGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLV--VEAW-DRTNSkklseGTLLSLDNQID 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 235 ESSGRVEVHAHVTNPEHRLVPGMFAKVSQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGE-KIEQRIVELGVNtNDGYVV 313
Cdd:PRK11556 285 ATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDEnKVSKHLVTPGIQ-DSQKVV 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 857909417 314 VEKGLKLGDNVVVTGQQNLKKASLVKVMNPNAEQKTVelitEPTSKENTQQTAE 367
Cdd:PRK11556 364 ISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE----EKATSREYAKKGA 413
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
50-348 |
2.67e-21 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 95.17 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 50 GKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSLALAKSKLKRVQELLKKQp 122
Cdd:PRK15030 58 GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPAtyqatydSAKGDLAKAQAAANIAQLTVNRYQKLLGTQ- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 123 dSMSQQDVEEL---GEQANLA--AADFRQKEALMN-DYLLV-APFDGQLTNFTHSVGSKIDS--ATALVSLIKLDPVEVQ 193
Cdd:PRK15030 137 -YISKQEYDQAladAQQANAAvtAAKAAVETARINlAYTKVtSPISGRIGKSNVTEGALVQNgqATALATVQQLDPIYVD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 194 YSIGQSD-------LGNAKLGQ-NVSIQVDAFVDEAF----SGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFAKV 261
Cdd:PRK15030 216 VTQSSNDflrlkqeLANGTLKQeNGKAKVSLITSDGIkfpqDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 262 SQMTSEDSTQMVVSQNSV-QAKDTERFVWVVNGE-KIEQRIVELGVNTNDGYVVVEkGLKLGDNVVVTGQQNLKKASLVK 339
Cdd:PRK15030 296 RLEEGLNPNAILVPQQGVtRTPRGDATVLVVGADdKVETRPIVASQAIGDKWLVTE-GLKAGDRVVISGLQKVRPGVQVK 374
|
....*....
gi 857909417 340 VMNPNAEQK 348
Cdd:PRK15030 375 AQEVTADNN 383
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
76-259 |
1.07e-19 |
|
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: 87.18 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 76 GDSVKKGELI----------AQLDNTKAKADLDKARSS--LALAKSKLKrvqeLLKkqpdsMSQQDVEELGeqanlaaad 143
Cdd:pfam16576 39 GDPVKKGQPLaelyspelvaAQQEYLLALRSGDALSKSelLRAARQRLR----LLG-----MPEAQIAELE--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 144 fRQKEALMNdYLLVAPFDGQLTNFTHSVGSKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFS 223
Cdd:pfam16576 101 -RTGKVQPT-VTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFE 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 857909417 224 GVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFA 259
Cdd:pfam16576 179 GKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
68-351 |
1.17e-16 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 81.30 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 68 ILNIHFKDGDSVKKGELIAQLDNTKAKADLDKARSSLALAKSKLKRVQELLKKQP-----DSMSQQDVEELGEQAN---- 138
Cdd:PRK09859 72 IIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQAsllktNYVSRQDYDTARTQLNeaea 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 139 ---LAAADFRQKEALMNDYLLVAPFDGQLTNFTHSVGSKI--DSATALVSLIKLDPVEVQYS------------IGQSDL 201
Cdd:PRK09859 152 nvtVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVtaNQADSLVTVQRLDPIYVDLTqsvqdflrmkeeVASGQI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 202 GNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHAHVTNPEHRLVPGMFakVSQMTSEDSTQ--MVVSQNSV 279
Cdd:PRK09859 232 KQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMY--VTALVDEGSRQnvLLVPQEGV 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 857909417 280 --QAKDTERFVWVVNGEKIEQRIVELGVNTNDGYVVVeKGLKLGDNVVVTGQQNLKKASLVKVMNPNAEQKTVE 351
Cdd:PRK09859 310 thNAQGKATALILDKDDVVQLREIEASKAIGDQWVVT-SGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTE 382
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
50-326 |
2.13e-15 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 77.51 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 50 GKIRATDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNTKAK--------------ADLDKARSSLALAKSKLKRVQ 115
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveatlmelrAQRQQAEAELKLARVTLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 116 ELLKKQpdSMSQQDVEELGEQANLAAADFRQKEALMN-------------DYL-LVAPFDGQLTNFTHSVGSKI---DSA 178
Cdd:PRK11578 134 RLAKTQ--AVSQQDLDTAATELAVKQAQIGTIDAQIKrnqasldtaktnlDYTrIVAPMAGEVTQITTLQGQTViaaQQA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 179 TALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDESSGRVEVHA--HVTNPEHRLVPG 256
Cdd:PRK11578 212 PNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYArfEVPNPNGLLRLD 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 857909417 257 MFAKVS-QMTSEDSTQMV-VSQNSVQAKDTERFVWVVNGEKIEQRIVELGVNtNDGYVVVEKGLKLGDNVVV 326
Cdd:PRK11578 292 MTAQVHiQLTDVKNVLTIpLSALGDPVGDNRYKVKLLRNGETREREVTIGAR-NDTDVEIVKGLEAGDEVII 362
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-326 |
4.19e-14 |
|
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: 72.84 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 40 QAFTSSINEVGKIRA-TDSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNTKAKADLDKARSSLALAKSKLKRVQELL 118
Cdd:pfam00529 2 APLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 119 KKQ-----PDSMSQQDVEELGEQANLAAADFRQKEA-------LMNDYLLVAPFDG----QLTNFTHSVGSkiDSATALV 182
Cdd:pfam00529 82 DRLqalesELAISRQDYDGATAQLRAAQAAVKAAQAqlaqaqiDLARRRVLAPIGGisreSLVTAGALVAQ--AQANLLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 183 SLIKLDPVEVQysIGQSDLGNAKLGQNVSIQVDAFVDEA-------------------FSGVVDYIAPAVDESSGRVEVH 243
Cdd:pfam00529 160 TVAQLDQIYVQ--ITQSAAENQAEVRSELSGAQLQIAEAeaelklakldlerteirapVDGTVAFLSVTVDGGTVSAGLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 244 AHVTNPEHRL-VPGMFA--KVSQMTSEDSTQMVvsQNSVQAKDTERF-VWVVN-GEKIEQRIVELGVnTNDGYVVVEKGL 318
Cdd:pfam00529 238 LMFVVPEDNLlVPGMFVetQLDQVRVGQPVLIP--FDAFPQTKTGRFtGVVVGiSPDTGPVRVVVDK-AQGPYYPLRIGL 314
|
....*...
gi 857909417 319 KLGDNVVV 326
Cdd:pfam00529 315 SAGALVRL 322
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
73-340 |
3.46e-13 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 70.59 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 73 FKDGDSVKKGELIAQLDNTKAKADLDKARSSLALAKS-------KLKRVQELLKKQpdSMSQQD-----VEELGEQANLA 140
Cdd:PRK09578 79 YEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAahlaaldKRRRYDDLVRDR--AVSERDyteavADERQAKAAVA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 141 AADFRQKEA-LMNDYLLV-APFDGQLTNFTHSVGSKI--DSATALVSLIKLDPVEVQYSIGQSD---LGNA-KLGQNVSI 212
Cdd:PRK09578 157 SAKAELARAqLQLDYATVtAPIDGRARRALVTEGALVgqDQATPLTTVEQLDPIYVNFSQPAADveaLRRAvKSGRATGI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 213 -QVDAFVDEAFSGVVDYIAP--------AVDESSGRVEVHAHVTNPEHRLVPGMFAKVSQMTSEDSTQMVVSQNSVQAKD 283
Cdd:PRK09578 237 aQQDVAVTLVRADGSEYPLKgkllfsdlAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 857909417 284 TERFVWVVNGEKIEQRiVELGVNT-NDGYVVVEKGLKLGDNVVVTGQQNLKKASLVKV 340
Cdd:PRK09578 317 DSASVKVVGQNGKVRD-VEVEADQmSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKA 373
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
76-328 |
9.21e-11 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 63.35 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 76 GDSVKKGELIAQL---DNTKAKADLDKARSSLALAkSKLKRVQELLKKQpdSMSQQDVEELgeqanlaaadfRQKEALMN 152
Cdd:PRK09783 143 GDKVQKGTPLLDLtipDWVEAQSEYLLLRETGGTA-TQTEGILERLRLA--GMPEADIRRL-----------IATRKIQT 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 153 DYLLVAPFDGQLTNFTHSVGSKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPA 232
Cdd:PRK09783 209 RFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 233 VDESSGRVEVHAHVTNPEHRLVPGMFAKVSQMTSEDSTQMVVSQNSVQAKDTERFVWVVNGEKIEQRIVELgVNTNDGYV 312
Cdd:PRK09783 289 VDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAV-FQESQGVT 367
|
250
....*....|....*.
gi 857909417 313 VVEKGLKLGDNVVVTG 328
Cdd:PRK09783 368 AIRSGLAEGEKVVSSG 383
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
156-249 |
3.66e-10 |
|
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: 56.99 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 156 LVAPFDGQLTNFTHSVGSKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAPAVDE 235
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVDP 81
|
90
....*....|....
gi 857909417 236 SSGRVEVHAHVTNP 249
Cdd:pfam13437 82 DTGVIPVRVSIENP 95
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
60-231 |
4.64e-10 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 60.75 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 60 LTFSASDKILNIHFKDGDSVKKGELIAQLDNT-------KAKADLDKARSSLAL-------------------------- 106
Cdd:PRK03598 46 LGFRVGGRLASLAVDEGDAVKAGQVLGELDAApyenalmQAKANVSVAQAQLDLmlagyrdeeiaqaraavkqaqaaydy 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857909417 107 AKSKLKRVQELLKKQpdSMSQQDV------------------------------EELGE-QANLAAADFRQKEALMN--D 153
Cdd:PRK03598 126 AQNFYNRQQGLWKSR--TISANDLenarssrdqaqatlksaqdklsqyregnrpQDIAQaKASLAQAQAALAQAELNlqD 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 857909417 154 YLLVAPFDGQLTNFTHSVGSKIDSATALVSLIKLDPVEVQYSIGQSDLGNAKLGQNVSIQVDAFVDEAFSGVVDYIAP 231
Cdd:PRK03598 204 TELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSP 281
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
56-105 |
3.14e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 35.50 E-value: 3.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 857909417 56 DSAALTFSASDKILNIHFKDGDSVKKGELIAQLDNTKAKADLDKARSSLA 105
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| |
