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Conserved domains on  [gi|15597689|ref|NP_251183|]
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resistance-nodulation-cell division (RND) multidrug efflux membrane fusion protein MexE [Pseudomonas aeruginosa PAO1]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
44-377 1.54e-86

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


:

Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 266.04  E-value: 1.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  44 VIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVN 123
Cdd:COG0845   3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 124 EAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGeTLLTT 203
Cdd:COG0845  83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLFT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 204 LVSTDKVYAYFDADERVFLKYvelarqagrdtRSESPVYLGLSSEDGNPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGE 283
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARL-----------KVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 284 FTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRV 363
Cdd:COG0845 231 LRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRL 310
                       330
                ....*....|....
gi 15597689 364 RPGMQVDPQKVEMA 377
Cdd:COG0845 311 RDGAKVRVVEAAAP 324
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
44-377 1.54e-86

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 266.04  E-value: 1.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  44 VIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVN 123
Cdd:COG0845   3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 124 EAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGeTLLTT 203
Cdd:COG0845  83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLFT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 204 LVSTDKVYAYFDADERVFLKYvelarqagrdtRSESPVYLGLSSEDGNPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGE 283
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARL-----------KVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 284 FTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRV 363
Cdd:COG0845 231 LRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRL 310
                       330
                ....*....|....
gi 15597689 364 RPGMQVDPQKVEMA 377
Cdd:COG0845 311 RDGAKVRVVEAAAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
39-369 7.40e-71

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: 225.66  E-value: 7.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689    39 VSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQ 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   119 ARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGE 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   199 TLLtTLVSTDKVYAYFDADERVFLKYvelarqagrdtRSESPVYLGLSSEDGNPHLGRLDFLDNQVNPRTGTIRGRAVFD 278
Cdd:TIGR01730 161 TLA-TIVDLDPLEADFSVPERDLPQL-----------RRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   279 NAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVN 358
Cdd:TIGR01730 229 NPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTA 308
                         330
                  ....*....|.
gi 15597689   359 GLQRVRPGMQV 369
Cdd:TIGR01730 309 GVVKLRDGAKV 319
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
46-357 9.88e-58

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: 191.87  E-value: 9.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689    46 EQPLNEWDEFTGRLEA-PESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVNE 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   125 AQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGE-TLLTT 203
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQaNLLAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   204 LVSTDKVYAYFDADERVFLKYVELARQAGRDTRSESPVYLGLSSEDG------NPHLGRLDFLDNQVNPRTGTIRGRAVF 277
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   278 DN-AKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVY-RTVEMGPKLEGLRIVRSGLSKGDRI 355
Cdd:pfam00529 241 VVpEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGpVRVVVDKAQGPYYPLRIGLSAGALV 320

                  ..
gi 15597689   356 VV 357
Cdd:pfam00529 321 RL 322
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
13-403 1.09e-49

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 172.98  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   13 LALAAVLVLSACGKAPETTQGMAAPKVSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLL 92
Cdd:PRK15030  14 LMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   93 FQIDPRPFEAEVKRLEAQLQQARAAQARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSF 172
Cdd:PRK15030  94 YQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  173 TRITAPIDGRVSRAEVTAGNLVNSGE-TLLTTLVSTDKVYAYFDADERVFLKY-VELARQAGRDTRSESPVYLGLSSEDG 250
Cdd:PRK15030 174 TKVTSPISGRIGKSNVTEGALVQNGQaTALATVQQLDPIYVDVTQSSNDFLRLkQELANGTLKQENGKAKVSLITSDGIK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  251 NPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVG-TDLGKKFVLVLDGDNKTV 329
Cdd:PRK15030 254 FPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVVGADDKVE 333
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597689  330 YRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRVRPGMQVDPQKVemaSADTlatlarlRQSVGDSEPPKVAAS 403
Cdd:PRK15030 334 TRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEV---TADN-------NQQAASGAQPEQSKS 397
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
44-377 1.54e-86

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 266.04  E-value: 1.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  44 VIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVN 123
Cdd:COG0845   3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 124 EAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGeTLLTT 203
Cdd:COG0845  83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLFT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 204 LVSTDKVYAYFDADERVFLKYvelarqagrdtRSESPVYLGLSSEDGNPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGE 283
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARL-----------KVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 284 FTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRV 363
Cdd:COG0845 231 LRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRL 310
                       330
                ....*....|....
gi 15597689 364 RPGMQVDPQKVEMA 377
Cdd:COG0845 311 RDGAKVRVVEAAAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
39-369 7.40e-71

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: 225.66  E-value: 7.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689    39 VSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQ 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   119 ARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGE 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   199 TLLtTLVSTDKVYAYFDADERVFLKYvelarqagrdtRSESPVYLGLSSEDGNPHLGRLDFLDNQVNPRTGTIRGRAVFD 278
Cdd:TIGR01730 161 TLA-TIVDLDPLEADFSVPERDLPQL-----------RRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   279 NAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVN 358
Cdd:TIGR01730 229 NPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTA 308
                         330
                  ....*....|.
gi 15597689   359 GLQRVRPGMQV 369
Cdd:TIGR01730 309 GVVKLRDGAKV 319
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
46-357 9.88e-58

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: 191.87  E-value: 9.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689    46 EQPLNEWDEFTGRLEA-PESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVNE 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   125 AQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGE-TLLTT 203
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQaNLLAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   204 LVSTDKVYAYFDADERVFLKYVELARQAGRDTRSESPVYLGLSSEDG------NPHLGRLDFLDNQVNPRTGTIRGRAVF 277
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   278 DN-AKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVY-RTVEMGPKLEGLRIVRSGLSKGDRI 355
Cdd:pfam00529 241 VVpEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGpVRVVVDKAQGPYYPLRIGLSAGALV 320

                  ..
gi 15597689   356 VV 357
Cdd:pfam00529 321 RL 322
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
13-403 1.09e-49

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 172.98  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   13 LALAAVLVLSACGKAPETTQGMAAPKVSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLL 92
Cdd:PRK15030  14 LMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   93 FQIDPRPFEAEVKRLEAQLQQARAAQARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSF 172
Cdd:PRK15030  94 YQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  173 TRITAPIDGRVSRAEVTAGNLVNSGE-TLLTTLVSTDKVYAYFDADERVFLKY-VELARQAGRDTRSESPVYLGLSSEDG 250
Cdd:PRK15030 174 TKVTSPISGRIGKSNVTEGALVQNGQaTALATVQQLDPIYVDVTQSSNDFLRLkQELANGTLKQENGKAKVSLITSDGIK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  251 NPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVG-TDLGKKFVLVLDGDNKTV 329
Cdd:PRK15030 254 FPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVVGADDKVE 333
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597689  330 YRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRVRPGMQVDPQKVemaSADTlatlarlRQSVGDSEPPKVAAS 403
Cdd:PRK15030 334 TRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEV---TADN-------NQQAASGAQPEQSKS 397
PRK09859 PRK09859
multidrug transporter subunit MdtE;
12-368 7.99e-46

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 162.19  E-value: 7.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   12 PLaLAAVLVLSACGKAPETTQGMAAPKVSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDL 91
Cdd:PRK09859  10 PL-LFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   92 LFQIDPRPFEAEVKRLEAQLQQARAAQARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLS 171
Cdd:PRK09859  89 LYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  172 FTRITAPIDGRVSRAEVTAGNLVNSGET-LLTTLVSTDKVYAYFDADERVFLKYV-ELARQAGRDTRSESPVYLGLSSED 249
Cdd:PRK09859 169 YANVTSPITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLTQSVQDFLRMKeEVASGQIKQVQGSTPVQLNLENGK 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  250 GNPHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDL-GKKFVLVLDGDNKT 328
Cdd:PRK09859 249 RYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAqGKATALILDKDDVV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 15597689  329 VYRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRVRPGMQ 368
Cdd:PRK09859 329 QLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIK 368
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
12-380 2.22e-42

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 153.03  E-value: 2.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   12 PLALAAVLVLSACGKAPETTQGMAAPKVSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDL 91
Cdd:PRK09578  11 LAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   92 LFQIDPRPFEAEVKRLEAQLQQARAAQARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLS 171
Cdd:PRK09578  91 LFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  172 FTRITAPIDGRVSRAEVTAGNLVNSGE-TLLTTLVSTDKVYAYFD---ADervflkyVELARQAGRDTR----SESPVYL 243
Cdd:PRK09578 171 YATVTAPIDGRARRALVTEGALVGQDQaTPLTTVEQLDPIYVNFSqpaAD-------VEALRRAVKSGRatgiAQQDVAV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  244 GLSSEDGN--PHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLV 321
Cdd:PRK09578 244 TLVRADGSeyPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKV 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597689  322 LDGDNKTVYRTVEMGPKLEGLRIVRSGLSKGDRIVVNGLQRVRPGMQVDPQKVEMASAD 380
Cdd:PRK09578 324 VGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAAKP 382
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
33-391 3.41e-40

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 148.01  E-value: 3.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   33 GMAAPKVSVAEVIEQPLNEWDEFTGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQ 112
Cdd:PRK11556  56 SGPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  113 QARAAQARSVNEAQRGERLRASNAISAELADARTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGN 192
Cdd:PRK11556 136 KDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGN 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  193 LVNSGETL-LTTLVSTDKVYAYFDADERVfLKYVELARQAGRDTRSEspvylglSSEDGNPHL---GRLDFLDNQVNPRT 268
Cdd:PRK11556 216 QISSGDTTgIVVITQTHPIDLVFTLPESD-IATVVQAQKAGKPLVVE-------AWDRTNSKKlseGTLLSLDNQIDATT 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  269 GTIRGRAVFDNAKGEFTPGLYVRLKLVGSKTYAATLIKDEAVGTDLGKKFVLVLDGDNKTVYRTVEMGPKLEGLRIVRSG 348
Cdd:PRK11556 288 GTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAG 367
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 15597689  349 LSKGDRIVVNGLQRVRPGMQVDpqKVEMASADTLATLARLRQS 391
Cdd:PRK11556 368 LSAGDRVVTDGIDRLTEGAKVE--VVEPQSATTPEEKATSREY 408
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
56-223 6.55e-20

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 89.72  E-value: 6.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  56 TGRLEApESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLE--------------------------- 108
Cdd:COG1566  38 DGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEaqlaaaeaqlarleaelgaeaeiaaae 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689 109 AQLQQARAAQARSVNEAQRGERLRASNAIS---------------AELADARTTAAQEAKAAVAATQA------------ 161
Cdd:COG1566 117 AQLAAAQAQLDLAQRELERYQALYKKGAVSqqeldearaaldaaqAQLEAAQAQLAQAQAGLREEEELaaaqaqvaqaea 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597689 162 QLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGETLLtTLVSTDKVY--AYFDADERVFLK 223
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLL-TIVPLDDLWveAYVPETDLGRVK 259
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
69-290 1.85e-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: 60.21  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689    69 PRVSGYIDRVAFH-EGALVKKGDLLFQID-PRPFEAEVKRLEAQLQQARAAQARSVNEAQrgERLRA---SNAISAELAD 143
Cdd:pfam16576  24 ARVEGWIEKLYVNaTGDPVKKGQPLAELYsPELVAAQQEYLLALRSGDALSKSELLRAAR--QRLRLlgmPEAQIAELER 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   144 ARTTAAqeakaavaatqaqldaarlnlSFTrITAPIDGRVSRAEVTAGNLVNSGETLLtTLVSTDKVYAYFDADERvflk 223
Cdd:pfam16576 102 TGKVQP---------------------TVT-VYAPISGVVTELNVREGMYVQPGDTLF-TIADLSTVWVEADVPEQ---- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597689   224 yvELAR-QAGRDTRSESPVYLGLSSEdgnphlGRLDFLDNQVNPRTGTIRGRAVFDNAKGEFTPGLYV 290
Cdd:pfam16576 155 --DLALvKVGQPAEVTLPALPGKTFE------GKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
56-194 5.98e-10

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 60.56  E-value: 5.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   56 TGRLEAPESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVNEA-------QRG 128
Cdd:PRK11578  53 TGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELklarvtlSRQ 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597689  129 ERLRASNAISAELADARTTAAQEAKAAVAATQAQ-------LDAARLNLSFTRITAPIDGRVSRAEVTAGNLV 194
Cdd:PRK11578 133 QRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQikrnqasLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTV 205
PRK10476 PRK10476
multidrug transporter subunit MdtN;
63-212 8.25e-10

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 60.04  E-value: 8.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   63 ESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEV-----------------KRL-----------EAQLQQA 114
Cdd:PRK10476  47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVaqaqadlaladaqimttQRSvdaersnaasaNEQVERA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  115 RAAQARSVNEAQRGERLRASNAISAE-LADART-----------------------TAAQEAKAAVAATQAQLDAARLNL 170
Cdd:PRK10476 127 RANAKLATRTLERLEPLLAKGYVSAQqVDQARTaqrdaevslnqallqaqaaaaavGGVDALVAQRAAREAALAIAELHL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15597689  171 SFTRITAPIDGRVSRAEVTAGNLVNSGETLLtTLVSTDKVYA 212
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQPIF-TLIDTDHWYA 247
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
65-215 1.03e-09

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 59.37  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   65 VELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLEAQLQQARAAQARSVNEAQRGERLRASnAISAELADA 144
Cdd:PRK10559  48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQ-AMSREEIDQ 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597689  145 RTTAAQEAKAAVAATQAQLDAARLNLSFTRITAPIDGRVSRAEVTAGNLVNSGETLLtTLVSTDKVY--AYFD 215
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAV-ALVKQNSFYvlAYME 198
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
63-108 2.86e-08

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 49.75  E-value: 2.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15597689    63 ESVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPFEAEVKRLE 108
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAE 46
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
28-360 6.60e-07

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 51.02  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   28 PETTQGMAapkVSVAEVIEQPLNEWDEFTGRLEAPES--VELRPRVSGYIDRV-AFHEGALVKKGDLLFQID-PRPFEAE 103
Cdd:PRK09783  88 PTQTQNLG---VKTATVTRGPLTFAQTFPANVSYNEYqyAIVQARAAGFIDKVyPLTVGDKVQKGTPLLDLTiPDWVEAQ 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  104 VKRLEAQLQQARAAQARSVNEaqrgeRLRASNAISAELADARTTAaqeakaavaatqaqldaaRLNLSFTrITAPIDGRV 183
Cdd:PRK09783 165 SEYLLLRETGGTATQTEGILE-----RLRLAGMPEADIRRLIATR------------------KIQTRFT-LKAPIDGVI 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  184 SRAEVTAGnlVNsgetllttlVSTDKVYAYFDADERVFLKYV---ELARQAGRDTRSE--SPVYlglssEDGNPHLGRLD 258
Cdd:PRK09783 221 TAFDLRAG--MN---------IAKDNVVAKIQGMDPVWVTAAipeSIAWLVKDASQFTltVPAR-----PDKTFTIRKWT 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  259 FLDNqVNPRTGTIRGRAVFDNAKGEFTPGLYVRLKLvGSKTYAATLIKDEAVgTDLGK-KFVLVLDGDNKTVYRTVEMGP 337
Cdd:PRK09783 285 LLPS-VDAATRTLQLRLEVDNADEALKPGMNAWLQL-NTASEPMLLIPSQAL-IDTGSeQRVITVDADGRFVPKRVAVFQ 361
                        330       340
                 ....*....|....*....|...
gi 15597689  338 KLEGLRIVRSGLSKGDRIVVNGL 360
Cdd:PRK09783 362 ESQGVTAIRSGLAEGEKVVSSGL 384
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
64-215 3.52e-06

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 48.42  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   64 SVELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPRPF-------EAEV--------KRLEAQLQQARAAQARSVNEAQ-- 126
Cdd:PRK03598  43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYenalmqaKANVsvaqaqldLMLAGYRDEEIAQARAAVKQAQaa 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  127 ---------RGERLRASNAISA-ELADARTTAAQEAKAAV-------------------------AATQAQLDAARLNLS 171
Cdd:PRK03598 123 ydyaqnfynRQQGLWKSRTISAnDLENARSSRDQAQATLKsaqdklsqyregnrpqdiaqakaslAQAQAALAQAELNLQ 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15597689  172 FTRITAPIDGRV-SRAeVTAGNLVNSGETLLtTLVSTDKVY--AYFD 215
Cdd:PRK03598 203 DTELIAPSDGTIlTRA-VEPGTMLNAGSTVF-TLSLTRPVWvrAYVD 247
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
174-287 1.00e-04

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 41.19  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   174 RITAPIDGRVSRAEVTAGNLVNSGETLLtTLVSTD--KVYAYFDADERVFLKyvelarqagrdtrSESPVYLGLSSEDGN 251
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLA-TIVPPDrlLVEAFVPAADLGSLK-------------KGQKVTLKLDPGSDY 66
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15597689   252 PHLGRLDFLDNQVNPRTGTIRGRAVFDNAKGE--FTPG 287
Cdd:pfam13437  67 TLEGKVVRISPTVDPDTGVIPVRVSIENPKTPipLLPG 104
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
65-201 7.13e-04

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 41.60  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689   65 VELRPRVSGYIDRVAFHEGALVKKGDLLFQIDPR----PFE-----------------AEVKRLEAQLQQARAAQARSVN 123
Cdd:PRK15136  62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTdaeqAFEkaktalansvrqthqlmINSKQYQANIELQKTALAQAQS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597689  124 EAQRGERLRASNAISAE-LADARTTAAQEAKaavaatqaQLDAAR--------------------------------LNL 170
Cdd:PRK15136 142 DLNRRVPLGNANLIGREeLQHARDAVASAQA--------QLDVAIqqynanqamilntpledqpavqqaatevrnawLAL 213
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15597689  171 SFTRITAPIDGRVSRAEVTAGNLVNSGETLL 201
Cdd:PRK15136 214 QRTKIVSPMTGYVSRRSVQVGAQISPTTPLM 244
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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