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Conserved domains on  [gi|527036768|ref|WP_020883509|]
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MULTISPECIES: p-hydroxybenzoic acid efflux pump subunit AaeA [Enterobacter]

Protein Classification

p-hydroxybenzoic acid efflux pump subunit AaeA( domain architecture ID 11484797)

p-hydroxybenzoic acid efflux pump subunit AaeA forms an efflux pump with AaeB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
1-310 0e+00

p-hydroxybenzoic acid efflux pump subunit AaeA;


:

Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 638.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   1 MKTLTRKISRTAITMALVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQ 80
Cdd:PRK10559   1 MKTLIRKISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  81 PRYQKALEEAEADVAYYQALASEKRREAGRRNQLGVQAMSREEIDQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAP 160
Cdd:PRK10559  81 PRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 161 ADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGFRAEITPLGSNRVLKGTVDSVAAGVTNSSSSN 240
Cdd:PRK10559 161 ADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTR 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 241 DTKGMATVDSNLEWVRLAQRVPVRIHLDEQQGNLWPAGTTATVVITGEKDRDASQDSIFRKIAHRLREFG 310
Cdd:PRK10559 241 DSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTTATVVITGKQDRDASQDSPFRKLAHRLREFG 310
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
1-310 0e+00

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 638.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   1 MKTLTRKISRTAITMALVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQ 80
Cdd:PRK10559   1 MKTLIRKISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  81 PRYQKALEEAEADVAYYQALASEKRREAGRRNQLGVQAMSREEIDQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAP 160
Cdd:PRK10559  81 PRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 161 ADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGFRAEITPLGSNRVLKGTVDSVAAGVTNSSSSN 240
Cdd:PRK10559 161 ADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTR 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 241 DTKGMATVDSNLEWVRLAQRVPVRIHLDEQQGNLWPAGTTATVVITGEKDRDASQDSIFRKIAHRLREFG 310
Cdd:PRK10559 241 DSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTTATVVITGKQDRDASQDSPFRKLAHRLREFG 310
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-285 1.27e-55

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 183.33  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   1 MKTLtrKISRTAITMALVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQ 80
Cdd:COG1566    1 MKAL--KKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  81 PRYQKALEEAEADVAYYQALASEKRREAGRRNQLGV----------------------------QAMSREEIDQ------ 126
Cdd:COG1566   79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAaeaqlaaaqaqldlaqreleryqalykkGAVSQQELDEaraald 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 127 ---------------------SNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVAL 185
Cdd:COG1566  159 aaqaqleaaqaqlaqaqaglrEEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 186 VKQNSFYVLAYMEETKLEGVRPGFRAEITPLG-SNRVLKGTVDSVAAGVTNSSSSNDTKGmatvdsnlewvRLAQRVPVR 264
Cdd:COG1566  239 VPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTSPPKNATG-----------NVVQRYPVR 307

                        330       340
                 ....*....|....*....|.
gi 527036768 265 IHLDEQQGNLWPAGTTATVVI 285
Cdd:COG1566  308 IRLDNPDPEPLRPGMSATVEI 328
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 31-285 4.30e-35

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: 129.47  E-value: 4.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   31 YYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQA----------- 99
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAqvarlqaeldr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  100 -----------------------------------LASEKRREAGRRNQLGVQAMSREEIDQSNNVLQTVLH-------- 136
Cdd:pfam00529  84 lqaleselaisrqdydgataqlraaqaavkaaqaqLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnllatvaq 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  137 ----------------------------QLAKAQATRDLARLDLERTVIRAPADGWITNLNVY-AGEFITRGSTAVALVK 187
Cdd:pfam00529 164 ldqiyvqitqsaaenqaevrselsgaqlQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  188 QNSFYVLAYMEETKLEGVRPGFRAEITPLGSNRVLKGTVDSVAAGVTnssssndtkgmatvdsnlewvrlAQRVPVRIHL 267
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGIS-----------------------PDTGPVRVVV 300

                         330       340
                  ....*....|....*....|
gi 527036768  268 DEQQGNLWP--AGTTATVVI 285
Cdd:pfam00529 301 DKAQGPYYPlrIGLSAGALV 320
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 46-293 1.12e-27

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: 109.33  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   46 DVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQL-GVQAMSREEI 124
Cdd:TIGR01730  25 DEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNAVSQADL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  125 DQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEG 204
Cdd:TIGR01730 105 DDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQ 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  205 VRPGFRAEITPLG-SNRVLKGTVDSVAAGVTNSSSSndtkgmatvdsnlewvrlaqrVPVRIHLDEQQGNLWPaGTTATV 283
Cdd:TIGR01730 185 LRRGQTLTVELDAlPGEEFKGKLRFIDPRVDSGTGT---------------------VRVRATFPNPDGRLLP-GMFGRV 242

                         250
                  ....*....|
gi 527036768  284 VITGEKDRDA 293
Cdd:TIGR01730 243 TISLKVRSSA 252
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
1-310 0e+00

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 638.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   1 MKTLTRKISRTAITMALVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQ 80
Cdd:PRK10559   1 MKTLIRKISRTAITLVLVILAFIAIFRAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  81 PRYQKALEEAEADVAYYQALASEKRREAGRRNQLGVQAMSREEIDQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAP 160
Cdd:PRK10559  81 PRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 161 ADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGFRAEITPLGSNRVLKGTVDSVAAGVTNSSSSN 240
Cdd:PRK10559 161 ADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTR 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 241 DTKGMATVDSNLEWVRLAQRVPVRIHLDEQQGNLWPAGTTATVVITGEKDRDASQDSIFRKIAHRLREFG 310
Cdd:PRK10559 241 DSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTTATVVITGKQDRDASQDSPFRKLAHRLREFG 310
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-285 1.27e-55

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 183.33  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   1 MKTLtrKISRTAITMALVILAFIAIFRAWVYYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQ 80
Cdd:COG1566    1 MKAL--KKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  81 PRYQKALEEAEADVAYYQALASEKRREAGRRNQLGV----------------------------QAMSREEIDQ------ 126
Cdd:COG1566   79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAaeaqlaaaqaqldlaqreleryqalykkGAVSQQELDEaraald 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 127 ---------------------SNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVAL 185
Cdd:COG1566  159 aaqaqleaaqaqlaqaqaglrEEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 186 VKQNSFYVLAYMEETKLEGVRPGFRAEITPLG-SNRVLKGTVDSVAAGVTNSSSSNDTKGmatvdsnlewvRLAQRVPVR 264
Cdd:COG1566  239 VPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTSPPKNATG-----------NVVQRYPVR 307

                        330       340
                 ....*....|....*....|.
gi 527036768 265 IHLDEQQGNLWPAGTTATVVI 285
Cdd:COG1566  308 IRLDNPDPEPLRPGMSATVEI 328
PRK10476 PRK10476
multidrug transporter subunit MdtN;
5-285 4.29e-44

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 153.64  E-value: 4.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   5 TRKISRTAITMALVILAFIAIFRAWVYY--TESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPR 82
Cdd:PRK10476   4 TPKKSPRKKLPALAIVALAIVALVFVIWrtDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  83 YQKALEEAEADVAYYQALASEKRR--EAGRRNQLGVQA---------------------------MSREEIDQSnnvlQT 133
Cdd:PRK10476  84 YELTVAQAQADLALADAQIMTTQRsvDAERSNAASANEqveraranaklatrtlerlepllakgyVSAQQVDQA----RT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 134 VLH----------------------------QLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVAL 185
Cdd:PRK10476 160 AQRdaevslnqallqaqaaaaavggvdalvaQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 186 VKQNSFYVLAYMEETKLEGVRPGFRAEITPL-GSNRVLKGTVDSVAAGVTNSSSSNDTKGMATVDSNLEWVRLAQRVPVR 264
Cdd:PRK10476 240 IDTDHWYAIANFRETDLKNIRVGDCATVYSMiDRGRPFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVR 319

                        330       340
                 ....*....|....*....|.
gi 527036768 265 IHLDEQQGNLWPAGTTATVVI 285
Cdd:PRK10476 320 IMLDKPDPELFRIGASAVVEL 340
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 46-293 7.11e-41

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: 144.70  E-value: 7.11e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  46 DVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQL-GVQAMSREEI 124
Cdd:COG0845   22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALlKKGAVSQQEL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 125 DQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEG 204
Cdd:COG0845  102 DQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLAR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 205 VRPGFRAEIT-PLGSNRVLKGTVDSVAAGVTNSSssndtkgmatvdsnlewvrlaQRVPVRIHLDEQQGNLWPaGTTATV 283
Cdd:COG0845  182 LKVGQPVTVTlDAGPGKTFEGKVTFIDPAVDPAT---------------------RTVRVRAELPNPDGLLRP-GMFVRV 239

                        250
                 ....*....|
gi 527036768 284 VITGEKDRDA 293
Cdd:COG0845  240 RIVLGERENA 249
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 31-285 4.30e-35

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: 129.47  E-value: 4.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   31 YYTESPWTRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQA----------- 99
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAqvarlqaeldr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  100 -----------------------------------LASEKRREAGRRNQLGVQAMSREEIDQSNNVLQTVLH-------- 136
Cdd:pfam00529  84 lqaleselaisrqdydgataqlraaqaavkaaqaqLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnllatvaq 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  137 ----------------------------QLAKAQATRDLARLDLERTVIRAPADGWITNLNVY-AGEFITRGSTAVALVK 187
Cdd:pfam00529 164 ldqiyvqitqsaaenqaevrselsgaqlQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  188 QNSFYVLAYMEETKLEGVRPGFRAEITPLGSNRVLKGTVDSVAAGVTnssssndtkgmatvdsnlewvrlAQRVPVRIHL 267
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGIS-----------------------PDTGPVRVVV 300

                         330       340
                  ....*....|....*....|
gi 527036768  268 DEQQGNLWP--AGTTATVVI 285
Cdd:pfam00529 301 DKAQGPYYPlrIGLSAGALV 320
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 46-293 1.12e-27

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: 109.33  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   46 DVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQL-GVQAMSREEI 124
Cdd:TIGR01730  25 DEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNAVSQADL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  125 DQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEG 204
Cdd:TIGR01730 105 DDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQ 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  205 VRPGFRAEITPLG-SNRVLKGTVDSVAAGVTNSSSSndtkgmatvdsnlewvrlaqrVPVRIHLDEQQGNLWPaGTTATV 283
Cdd:TIGR01730 185 LRRGQTLTVELDAlPGEEFKGKLRFIDPRVDSGTGT---------------------VRVRATFPNPDGRLLP-GMFGRV 242

                         250
                  ....*....|
gi 527036768  284 VITGEKDRDA 293
Cdd:TIGR01730 243 TISLKVRSSA 252
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
6-271 6.59e-23

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 97.46  E-value: 6.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   6 RKISRTAITMALVILAFIAIfrAWVYYtespW---------TRDARFSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLF 76
Cdd:PRK15136  17 KGKRKRALLLLTLLFIIIGV--AYGIY----WflvlrhhqeTDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  77 TIDQPRYQKALEEAEA--------------------------DVAYYQALASEKRREA-GRRNQLGVQ---------AMS 120
Cdd:PRK15136  91 TLDPTDAEQAFEKAKTalansvrqthqlminskqyqanielqKTALAQAQSDLNRRVPlGNANLIGREelqhardavASA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 121 REEID----QSNN----VLQTVL-HQLAKAQATRDL--ARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVALVKQN 189
Cdd:PRK15136 171 QAQLDvaiqQYNAnqamILNTPLeDQPAVQQAATEVrnAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPAT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 190 SFYVLAYMEETKLEGVRPGFRAEITP--LGSNRVLKGTVDSVAAGvTNSSSSNDTKGMATVDsnleWVRLAQRVPVRIHL 267
Cdd:PRK15136 251 NLWVDANFKETQLANMRIGQPATITSdiYGDDVVYTGKVVGLDMG-TGSAFSLLPAQNATGN----WIKVVQRLPVRIEL 325


                 ....
gi 527036768 268 DEQQ 271
Cdd:PRK15136 326 DAKQ 329
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
46-95 6.24e-15

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 67.85  E-value: 6.24e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 527036768   46 DVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVA 95
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
47-188 1.51e-11

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 64.35  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  47 VVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQL-GVQAMSREEID 125
Cdd:PRK15030  65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLlGTQYISKQEYD 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036768 126 QSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRG-STAVALVKQ 188
Cdd:PRK15030 145 QALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGqATALATVQQ 208
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 40-217 5.29e-11

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 62.87  E-value: 5.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  40 DARFSADVVAiapDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADV-----AYYQALASEK--RREAGRRN 112
Cdd:PRK11578  57 DALRKVDVGA---QVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLmelraQRQQAEAELKlaRVTLSRQQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 113 QL-GVQAMSREEIDQSNNVLQ-------TVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTA-- 182
Cdd:PRK11578 134 RLaKTQAVSQQDLDTAATELAvkqaqigTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQApn 213

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 527036768 183 -VALVKQNSFYVLAYMEETKLEGVRPGFRAEITPLG 217
Cdd:PRK11578 214 iLTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLG 249
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 46-229 1.86e-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: 59.44  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   46 DVVAIAPDVAGLITAVNVHDN-QLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRrNQLGVQAMSREEI 124
Cdd:pfam16576  18 RLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKSELLRAAR-QRLRLLGMPEAQI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  125 DQsnnvlqtvlhqLAKAQATRdlarldlERTVIRAPADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEG 204
Cdd:pfam16576  97 AE-----------LERTGKVQ-------PTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLAL 158

                         170       180
                  ....*....|....*....|....*.
gi 527036768  205 VRPGFRAEIT-PLGSNRVLKGTVDSV 229
Cdd:pfam16576 159 VKVGQPAEVTlPALPGKTFEGKVDYI 184
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
44-186 9.54e-10

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 59.03  E-value: 9.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  44 SADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQLG-VQAMSRE 122
Cdd:PRK11556  84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAkTNLVSRQ 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036768 123 EIDQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVALV 186
Cdd:PRK11556 164 ELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVV 227
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 9-226 1.98e-09

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 57.66  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   9 SRTAITMALVILAFIAIFRAWVYYTESPwTRDARFSADV----VAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQ 84
Cdd:PRK03598   2 KKKVVIGLAVVVLAAAVAGGWWWYQSRQ-DNGLTLYGNVdirtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  85 KALEEAEADV------------------------AYYQALA---------------------SEKRREAGR--RNQ--LG 115
Cdd:PRK03598  81 NALMQAKANVsvaqaqldlmlagyrdeeiaqaraAVKQAQAaydyaqnfynrqqglwksrtiSANDLENARssRDQaqAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768 116 VQAM----------SR-EEIDQSNNvlqtvlhQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGSTAVA 184
Cdd:PRK03598 161 LKSAqdklsqyregNRpQDIAQAKA-------SLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFT 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 527036768 185 LVKQNSFYVLAYMEETKLEGVRPGFRAEITPLG-SNRVLKGTV 226
Cdd:PRK03598 234 LSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGrPDKPYHGQI 276
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 156-238 2.10e-07

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: 48.51  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  156 VIRAPADGWITNLNVYAGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGFRAEIT-PLGSNRVLKGTVDSVAAGVT 234
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKlDPGSDYTLEGKVVRISPTVD 80


                  ....
gi 527036768  235 NSSS 238
Cdd:pfam13437  81 PDTG 84
PRK09859 PRK09859
multidrug transporter subunit MdtE;
46-193 6.16e-06

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 47.40  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  46 DVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQALASEKRREAGRRNQ-LGVQAMSREEI 124
Cdd:PRK09859  60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASlLKTNYVSRQDY 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036768 125 DQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADGWITNLNVYAGEFIT--RGSTAVALVKQNSFYV 193
Cdd:PRK09859 140 DTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTanQADSLVTVQRLDPIYV 210
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 84-289 2.70e-05

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 45.39  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   84 QKALEEAEADVAYYQALASEKRREAG--RRNQLGVQAMSREEIDQSNNVLQTvlhQLAKAQATRDLARLDLERTVIRAPA 161
Cdd:TIGR01843 202 ERERAEAQGELGRLEAELEVLKRQIDelQLERQQIEQTFREEVLEELTEAQA---RLAELRERLNKARDRLQRLIIRSPV 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  162 DGWITNLNVY-AGEFITRGSTAVALVKQN-SFYVLAYMEETKLEGVRPGFRAEIT----PLGSNRVLKGTVDSVAAgvtn 235
Cdd:TIGR01843 279 DGTVQSLKVHtVGGVVQPGETLMEIVPEDdPLEIEAKLSPKDIGFVHVGQPAEIKfsafPYRRYGILNGKVKSISP---- 354

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036768  236 sSSSNDTKGMATVdsnlewvrlaqrVPVRIHLDE-------QQGNLWPaGTTATV-VITGEK 289
Cdd:TIGR01843 355 -DTFTDERGGGPY------------YRVRISIDQntlgigpKGLELSP-GMPVTAdIKTGER 402
NHLM_micro_HlyD TIGR03794
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the ...
 16-285 4.02e-05

NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the HlyD membrane fusion protein of type I secretion systems. Their occurrence in prokaryotic genomes is associated with the occurrence of a novel class of microcin (small bacteriocins) with a leader peptide region related to nitrile hydratase. We designate the class of bacteriocin as Nitrile Hydratase Leader Microcin, or NHLM. This family, therefore, is designated as NHLM bacteriocin system secretion protein. Some but not all NHLM-class putative microcins belong to the TOMM (thiazole/oxazole modified microcin) class as assessed by the presence of the scaffolding protein and/or cyclodehydratase in the same gene clusters. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274787 [Multi-domain]  Cd Length: 421  Bit Score: 44.84  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   16 ALVILAFIAIF---RAWVYYTESPWTRDAR----FSADVVAIAPDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALE 88
Cdd:TIGR03794  20 WLALAALGVIVvaaLAWGIFGSIPITVSGNgiliLSSGVDTIQSPGSGVVIDLDVEVGDQVKKGQVVARLFQPELRERLQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   89 EAEADVAYYQALASEKRR------EAGRRNQLGVQAMSRE--------------EIDQSNNVLQTVLHQLAKA------- 141
Cdd:TIGR03794 100 ESYQKLTQLQEQLEEVRNytgrlkEGRERHFQKSKEALEEtigrlreelaalsrEVGKQRGLLSRGLATFKRDrilqqqw 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  142 ----------------------------------------------------------QATRDLARLDLE---RTVIRAP 160
Cdd:TIGR03794 180 reeqakydaadkaraiyalqtkadernletvlqslsqadfqlagvaqqeletvearikEARYEIEELENKlnlNTRIVSQ 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  161 ADGWITNLNVYAGEFITRGSTAVALVKQNSFY----VLAYMEETKLEGVRPGFRAEITPLGSNR----VLKGTVDSVaag 232
Cdd:TIGR03794 260 HSGRVIELNYTPGQLVAAGAPLASLEVEDQTDegleGVAYFPVAEGKKIRPGMSVQITPSTVKAerdgYIRGTVTSV--- 336

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036768  233 vtnSSSSNDTKGMATVDSNLEWVR--LAQRVPVRIHLDEQQ------GNLWPAGTTATVVI 285
Cdd:TIGR03794 337 ---SEYPATKEAMDRTLGNEAFVQylLAQGPPIEVFVALERdrsspsGFKWSSGSGPDIKI 394
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
34-163 2.49e-04

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 42.47  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768  34 ESPWTRDARFSADVVAiapDVAGLITAVNVHDNQLVKKDQVLFTIDQPRYQKALEEAEADVAYYQA---LASEKRREagR 110
Cdd:PRK09578  53 ELPGRLDAYRQAEVRA---RVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAahlAALDKRRR--Y 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 527036768 111 RNQLGVQAMSREEIDQSNNVLQTVLHQLAKAQATRDLARLDLERTVIRAPADG 163
Cdd:PRK09578 128 DDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDG 180
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 9-180 2.82e-03

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 39.22  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768    9 SRTAITMALVILAFIAIFRAWVYYTEspwtrdarfsADVVAIA--------------PDVAGLITAVNVHDNQLVKKDQV 74
Cdd:TIGR01843   1 SRFARLITWLIAGLVVIFFLWAYFAP----------LDVVATAtgkvvpsgnvkvvqHLEGGIVREILVREGDRVKAGQV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036768   75 LFTIDQPRYQKALEE-------AEADVAYYQALASEkrREAGRRNQLGVQA---MSREEIDQSNNVLQTVL--HQLAKAQ 142
Cdd:TIGR01843  71 LVELDATDVEADAAElesqvlrLEAEVARLRAEADS--QAAIEFPDDLLSAedpAVPELIKGQQSLFESRKstLRAQLEL 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 527036768  143 ATRDLARLDLERTVIRAPADGWITNLNVYAGEFITRGS 180
Cdd:TIGR01843 149 ILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRK 186
 
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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