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Conserved domains on  [gi|499254856|ref|WP_010952396|]
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MULTISPECIES: HlyD family secretion protein [Pseudomonas]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

HlyD family secretion protein similar to Escherichia coli protein YhiI, Acinetobacter baumannii colistin resistance protein EmrA, and Burkholderia cepacia fusaric acid resistance protein FusE

Gene Ontology:  GO:0022857|GO:0016020|GO:0055085
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10559 super family cl32535
p-hydroxybenzoic acid efflux pump subunit AaeA;
8-281 1.70e-72

p-hydroxybenzoic acid efflux pump subunit AaeA;


The actual alignment was detected with superfamily member PRK10559:

Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 225.01  E-value: 1.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   8 IATLLVLVAAVAIGRqLWLHYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAK 87
Cdd:PRK10559  13 ITLVLVILAFIAIFR-AWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  88 ALVASRKATWEMRKVNAKRRADMDNLVISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIH 167
Cdd:PRK10559  92 ADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 168 KGDYARTGEAVMAVVDENSFWVYGFFEETKLPHVKVGDQAELQMMSGER-LKGHVESIARGIYDRDNPQSRELIADVNPT 246
Cdd:PRK10559 172 TGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKvLKGTVDSVAAGVTNSSSTRDSKGMATIDSN 251

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 499254856 247 FNWVRLAQRVPVRIHIDEVPeGFLLAAGTTCTVVV 281
Cdd:PRK10559 252 LEWVRLAQRVPVRIRLDNQQ-GNLYPAGTTATVVI 285
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
8-281 1.70e-72

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 225.01  E-value: 1.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   8 IATLLVLVAAVAIGRqLWLHYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAK 87
Cdd:PRK10559  13 ITLVLVILAFIAIFR-AWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  88 ALVASRKATWEMRKVNAKRRADMDNLVISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIH 167
Cdd:PRK10559  92 ADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 168 KGDYARTGEAVMAVVDENSFWVYGFFEETKLPHVKVGDQAELQMMSGER-LKGHVESIARGIYDRDNPQSRELIADVNPT 246
Cdd:PRK10559 172 TGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKvLKGTVDSVAAGVTNSSSTRDSKGMATIDSN 251

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 499254856 247 FNWVRLAQRVPVRIHIDEVPeGFLLAAGTTCTVVV 281
Cdd:PRK10559 252 LEWVRLAQRVPVRIRLDNQQ-GNLYPAGTTATVVI 285
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
11-284 5.94e-61

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 196.04  E-value: 5.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  11 LLVLVAAVAIGRQLWLHYM---TTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAK 87
Cdd:COG1566   10 LALVLLLLALGLALWAAGRngpDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  88 ALVASRKATWEMRKVNAKRRADMDNL----------------------------VISKENRDDASNIANSAQADYQQALA 139
Cdd:COG1566   90 AQLAAAEAQLARLEAELGAEAEIAAAeaqlaaaqaqldlaqreleryqalykkgAVSQQELDEARAALDAAQAQLEAAQA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 140 ELAAAE---------------------------LNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYGF 192
Cdd:COG1566  170 QLAQAQaglreeeelaaaqaqvaqaeaalaqaeLNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAY 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 193 FEETKLPHVKVGDQAELQMMS--GERLKGHVESIARGIYDRDNPQsreliadvNPTFNwvrLAQRVPVRIHIDEvPEGFL 270
Cdd:COG1566  250 VPETDLGRVKPGQPVEVRVDAypDRVFEGKVTSISPGAGFTSPPK--------NATGN---VVQRYPVRIRLDN-PDPEP 317

                        330
                 ....*....|....
gi 499254856 271 LAAGTTCTVVVKPG 284
Cdd:COG1566  318 LRPGMSATVEIDTE 331
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
 2-263 7.55e-39

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 138.77  E-value: 7.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856    2 KKFFSLIATLLVLVAAVAIGRQLWLHYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQL 81
Cdd:TIGR00998   1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   82 AVDQAKALVAS--RKATWEMRKVN-----------------AKRRADMDNL----------VISKENRDDASNIANSAQA 132
Cdd:TIGR00998  81 ALAKAEANLAAlvRQTKQLEITVQqlqakveslkikleqarEKLLQAELDLrrrvplfkkgLISREELDHARKALLSAKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  133 DY--------------------------QQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENS 186
Cdd:TIGR00998 161 ALnaaiqeqlnanqalvrgtplkkqpavQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  187 FWVYGFFEETKLPHVKVGDQAELQM-MSGERLK--GHVESIARGiydrdNPQSRELIADVNPTFNWVRLAQRVPVRIHID 263
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSdLYGSDVVfeGKVTGISMG-----TGSAFSLLPAQNATGNWIKVVQRLPVRIKLD 315
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 27-228 1.04e-23

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: 98.26  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   27 HYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKAT---------- 96
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQvarlqaeldr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   97 WEM-----------------------RKVNAKRRA--------------------------DMDNLVIS----------- 116
Cdd:pfam00529  84 LQAleselaisrqdydgataqlraaqAAVKAAQAQlaqaqidlarrrvlapiggisreslvTAGALVAQaqanllatvaq 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  117 ------------KENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIH-KGDYARTGEAVMAVVD 183
Cdd:pfam00529 164 ldqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVP 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 499254856  184 ENSFWVYGFFEETKLPHVKVGDQAEL-QMMSGERLKGHVESIARGI 228
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIpFDAFPQTKTGRFTGVVVGI 289
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 46-74 5.88e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.70  E-value: 5.88e-03
                         10        20
                 ....*....|....*....|....*....
gi 499254856  46 VAADVPGYVVDVPVKDNQRVKKGDLLIQI 74
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVL 30
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
8-281 1.70e-72

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 225.01  E-value: 1.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   8 IATLLVLVAAVAIGRqLWLHYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAK 87
Cdd:PRK10559  13 ITLVLVILAFIAIFR-AWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  88 ALVASRKATWEMRKVNAKRRADMDNLVISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIH 167
Cdd:PRK10559  92 ADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 168 KGDYARTGEAVMAVVDENSFWVYGFFEETKLPHVKVGDQAELQMMSGER-LKGHVESIARGIYDRDNPQSRELIADVNPT 246
Cdd:PRK10559 172 TGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKvLKGTVDSVAAGVTNSSSTRDSKGMATIDSN 251

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 499254856 247 FNWVRLAQRVPVRIHIDEVPeGFLLAAGTTCTVVV 281
Cdd:PRK10559 252 LEWVRLAQRVPVRIRLDNQQ-GNLYPAGTTATVVI 285
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
11-284 5.94e-61

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 196.04  E-value: 5.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  11 LLVLVAAVAIGRQLWLHYM---TTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAK 87
Cdd:COG1566   10 LALVLLLLALGLALWAAGRngpDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  88 ALVASRKATWEMRKVNAKRRADMDNL----------------------------VISKENRDDASNIANSAQADYQQALA 139
Cdd:COG1566   90 AQLAAAEAQLARLEAELGAEAEIAAAeaqlaaaqaqldlaqreleryqalykkgAVSQQELDEARAALDAAQAQLEAAQA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 140 ELAAAE---------------------------LNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYGF 192
Cdd:COG1566  170 QLAQAQaglreeeelaaaqaqvaqaeaalaqaeLNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAY 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 193 FEETKLPHVKVGDQAELQMMS--GERLKGHVESIARGIYDRDNPQsreliadvNPTFNwvrLAQRVPVRIHIDEvPEGFL 270
Cdd:COG1566  250 VPETDLGRVKPGQPVEVRVDAypDRVFEGKVTSISPGAGFTSPPK--------NATGN---VVQRYPVRIRLDN-PDPEP 317

                        330
                 ....*....|....
gi 499254856 271 LAAGTTCTVVVKPG 284
Cdd:COG1566  318 LRPGMSATVEIDTE 331
PRK10476 PRK10476
multidrug transporter subunit MdtN;
2-286 1.28e-51

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 172.52  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   2 KKFFSLIATLLVLVAAVAIGRQLWLHymttPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQL 81
Cdd:PRK10476  11 KKLPALAIVALAIVALVFVIWRTDSA----PSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  82 AVDQAKALVASRKATWEMRK--VNAKR-----------RAD------------MDNLV----ISKENRDDASNIANSAQA 132
Cdd:PRK10476  87 TVAQAQADLALADAQIMTTQrsVDAERsnaasaneqveRARanaklatrtlerLEPLLakgyVSAQQVDQARTAQRDAEV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 133 DYQQALAELAAAEL------------------------NLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFW 188
Cdd:PRK10476 167 SLNQALLQAQAAAAavggvdalvaqraareaalaiaelHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWY 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 189 VYGFFEETKLPHVKVGDQAELQMMS--GERLKGHVESIARGIYDRDNPQSRELIADVNPTFNWVRLAQRVPVRIHIDEVP 266
Cdd:PRK10476 247 AIANFRETDLKNIRVGDCATVYSMIdrGRPFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDKPD 326

                        330       340
                 ....*....|....*....|
gi 499254856 267 EGfLLAAGTTCTVVVKPGEG 286
Cdd:PRK10476 327 PE-LFRIGASAVVELRPGAA 345
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 37-271 2.82e-39

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: 139.69  E-value: 2.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  37 GRVRAD-IINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKATWEMRKVNAKRRADM-DNLV 114
Cdd:COG0845   16 GTVEARrEVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALlKKGA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 115 ISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYGFFE 194
Cdd:COG0845   96 VSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 195 ETKLPHVKVGDQAELQM--MSGERLKGHVESIARGIydrdNPQSRELIADV---NPTFNWvRLAQRVPVRIHIDEVPEGF 269
Cdd:COG0845  176 ESDLARLKVGQPVTVTLdaGPGKTFEGKVTFIDPAV----DPATRTVRVRAelpNPDGLL-RPGMFVRVRIVLGERENAL 250


                 ..
gi 499254856 270 LL 271
Cdd:COG0845  251 LV 252
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
 2-263 7.55e-39

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 138.77  E-value: 7.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856    2 KKFFSLIATLLVLVAAVAIGRQLWLHYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQL 81
Cdd:TIGR00998   1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   82 AVDQAKALVAS--RKATWEMRKVN-----------------AKRRADMDNL----------VISKENRDDASNIANSAQA 132
Cdd:TIGR00998  81 ALAKAEANLAAlvRQTKQLEITVQqlqakveslkikleqarEKLLQAELDLrrrvplfkkgLISREELDHARKALLSAKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  133 DY--------------------------QQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENS 186
Cdd:TIGR00998 161 ALnaaiqeqlnanqalvrgtplkkqpavQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  187 FWVYGFFEETKLPHVKVGDQAELQM-MSGERLK--GHVESIARGiydrdNPQSRELIADVNPTFNWVRLAQRVPVRIHID 263
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSdLYGSDVVfeGKVTGISMG-----TGSAFSLLPAQNATGNWIKVVQRLPVRIKLD 315
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 37-225 5.26e-26

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: 104.32  E-value: 5.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   37 GRVRA-DIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKATWEMRKVNAKRRADM-DNLV 114
Cdd:TIGR01730  19 GSLEAvDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvKRNA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  115 ISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYGFFE 194
Cdd:TIGR01730  99 VSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVP 178

                         170       180       190
                  ....*....|....*....|....*....|...
gi 499254856  195 ETKLPHVKVG--DQAELQMMSGERLKGHVESIA 225
Cdd:TIGR01730 179 ERDLPQLRRGqtLTVELDALPGEEFKGKLRFID 211
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 27-228 1.04e-23

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: 98.26  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   27 HYMTTPWTRDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKAT---------- 96
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQvarlqaeldr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   97 WEM-----------------------RKVNAKRRA--------------------------DMDNLVIS----------- 116
Cdd:pfam00529  84 LQAleselaisrqdydgataqlraaqAAVKAAQAQlaqaqidlarrrvlapiggisreslvTAGALVAQaqanllatvaq 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  117 ------------KENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIH-KGDYARTGEAVMAVVD 183
Cdd:pfam00529 164 ldqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVP 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 499254856  184 ENSFWVYGFFEETKLPHVKVGDQAEL-QMMSGERLKGHVESIARGI 228
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIpFDAFPQTKTGRFTGVVVGI 289
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
2-264 5.50e-23

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 97.07  E-value: 5.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   2 KKFFSLIATLLVLVAAVAIGRQLWL---HYMTTPwtrDGRVRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEH 78
Cdd:PRK15136  20 RKRALLLLTLLFIIIGVAYGIYWFLvlrHHQETD---DAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  79 YQLAVDQAKALVASR--------------KATWEMRKV-------NAKRRADMDNL-VISKENRDDASNIANSAQADY-- 134
Cdd:PRK15136  97 AEQAFEKAKTALANSvrqthqlminskqyQANIELQKTalaqaqsDLNRRVPLGNAnLIGREELQHARDAVASAQAQLdv 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856 135 -----------------------QQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYG 191
Cdd:PRK15136 177 aiqqynanqamilntpledqpavQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDA 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499254856 192 FFEETKLPHVKVGDQAELQM-MSGERL--KGHVESIargiyDRDNPQSRELIADVNPTFNWVRLAQRVPVRIHIDE 264
Cdd:PRK15136 257 NFKETQLANMRIGQPATITSdIYGDDVvyTGKVVGL-----DMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDA 327
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
44-91 1.30e-14

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 66.70  E-value: 1.30e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 499254856   44 INVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVA 91
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 37-270 2.35e-14

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: 70.23  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   37 GRVRAD---IINVAADVPGYVVDVPVKDN-QRVKKGDLLIQID-PEHYQLAVDQAKALVASRKATWEMRKVNAKRR---A 108
Cdd:pfam16576  10 GRVAYDerrLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYsPELVAAQQEYLLALRSGDALSKSELLRAARQRlrlL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  109 DMDNLVISKenrddasnIANSAQAdyqqalaelaaaelnLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFW 188
Cdd:pfam16576  90 GMPEAQIAE--------LERTGKV---------------QPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVW 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  189 VYGFFEETKLPHVKVGDQAELQM--MSGERLKGHVESiargIYDRDNPQSReliadvnpTfnwvrlaqrVPVRIHIDEvP 266
Cdd:pfam16576 147 VEADVPEQDLALVKVGQPAEVTLpaLPGKTFEGKVDY----IYPTLDPKTR--------T---------VRVRIELPN-P 204


                  ....
gi 499254856  267 EGFL 270
Cdd:pfam16576 205 DGRL 208
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 1-101 7.73e-10

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 58.82  E-value: 7.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856   1 MKKFFSLIATLLVLVAAVAIGRQLWLHYMTTPWTRDGRVraDI--INVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEH 78
Cdd:PRK03598   1 MKKKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLYGNV--DIrtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAP 78

                         90       100
                 ....*....|....*....|...
gi 499254856  79 YQLAVDQAKALVASRKATWEMRK 101
Cdd:PRK03598  79 YENALMQAKANVSVAQAQLDLML 101
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
41-182 5.00e-07

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 50.56  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  41 ADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKATWemrkVNAKRR-ADMDNLV----I 115
Cdd:PRK11556  85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATL----ANARRDlARYQQLAktnlV 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499254856 116 SKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEAVMAVV 182
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVV 227
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
37-184 5.48e-07

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 50.48  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  37 GRVRA-DIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKATWEMRKVNAKRRADM-DNLV 114
Cdd:PRK15030  58 GRTSAyRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLlGTQY 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499254856 115 ISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDGYVTNLNIHKGDYARTGEA-VMAVVDE 184
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQAtALATVQQ 208
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 153-233 5.65e-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: 46.97  E-value: 5.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  153 IVATVDGYVTNLNIHKGDYARTGEAVMAVVDENSFWVYGFFEETKLPHVKVGDQAELQMMSGE--RLKGHVESIARGIYD 230
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSdyTLEGKVVRISPTVDP 81


                  ...
gi 499254856  231 RDN 233
Cdd:pfam13437  82 DTG 84
PRK09859 PRK09859
multidrug transporter subunit MdtE;
37-159 2.43e-06

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 48.17  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  37 GR-VRADIINVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKALVASRKATWEMRKVNAKRRAD-MDNLV 114
Cdd:PRK09859  54 GRtVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASlLKTNY 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499254856 115 ISKENRDDASNIANSAQADYQQALAELAAAELNLKRTHIVATVDG 159
Cdd:PRK09859 134 VSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITG 178
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 44-169 8.81e-04

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 40.53  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254856  44 INVAADVPGYVVDVPVKDNQRVKKGDLLIQIDPEHYQLAVDQAKA----LVASR---KATWEMRKVNAKRRADMDNL-VI 115
Cdd:PRK11578  62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEAtlmeLRAQRqqaEAELKLARVTLSRQQRLAKTqAV 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499254856 116 SKENRDDASNIANSAQA-----DYQ--QALAELAAAELNLKRTHIVATVDGYVTNLNIHKG 169
Cdd:PRK11578 142 SQQDLDTAATELAVKQAqigtiDAQikRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQG 202
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 38-74 5.59e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 38.14  E-value: 5.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499254856   38 RVRADIIN---VAADVPGYVVDVPVKDNQRVKKGDLLIQI 74
Cdd:COG1038  1068 REKADPGNpghIGAPMPGTVVKVLVKEGDEVKKGDPLLTI 1107
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 46-74 5.88e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.70  E-value: 5.88e-03
                         10        20
                 ....*....|....*....|....*....
gi 499254856  46 VAADVPGYVVDVPVKDNQRVKKGDLLIQI 74
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVL 30
 
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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