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Conserved domains on  [gi|15829798|ref|NP_308571|]
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membrane fusion protein of a transport system [Escherichia coli O157:H7 str. Sakai]

Protein Classification

putative HlyD family type I secretion protein( domain architecture ID 1000742)

putative HlyD family type I secretion protein similar to Escherichia coli hemolysin secretion protein D, an inner membrane protein involved in the transport of hemolysin A

Gene Ontology:  GO:0016020|GO:0005886|GO:0009306
TCDB:  8.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
14-391 4.63e-99

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.


The actual alignment was detected with superfamily member TIGR01843:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 423  Bit Score: 300.77  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    14 PRLPRsaLAVRVTAVMLLCFLGWAWYFQLDEVTTGSGTVEPSGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTK 93
Cdd:TIGR01843   1 SRFAR--LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    94 TESDVQEAMSRLYAALATSARLRAEVSNKPL-VFPDEL-----NKFPELIESETALYNTRR------------------- 148
Cdd:TIGR01843  79 VEADAAELESQVLRLEAEVARLRAEADSQAAiEFPDDLlsaedPAVPELIKGQQSLFESRKstlraqlelilaqikqlea 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   149 --DGLNKATTGLTQGISLVNRELAMTQPLVKQGAASSVEVLRLQR---------------------QANELENKLSDVRT 205
Cdd:TIGR01843 159 elAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELEReraeaqgelgrleaelevlkrQIDELQLERQQIEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   206 QYYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVTTVGGVIAPGGKLMTIVPLDEQLLIEAKISP 285
Cdd:TIGR01843 239 TFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   286 RDVAFIHPGQKSLVKITAYDYSIYGGLPGEVAVISPDTVQDEVRRDVyYYRVYIRTFSNHLENKsKQQFPIFPGMVATVD 365
Cdd:TIGR01843 319 KDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGP-YYRVRISIDQNTLGIG-PKGLELSPGMPVTAD 396
                         410       420
                  ....*....|....*....|....*..
gi 15829798   366 IRTGKKSVLDYLLKPFNKA-QEALRER 391
Cdd:TIGR01843 397 IKTGERTVIEYLLKPITDSvQEALRER 423
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
14-391 4.63e-99

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: 300.77  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    14 PRLPRsaLAVRVTAVMLLCFLGWAWYFQLDEVTTGSGTVEPSGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTK 93
Cdd:TIGR01843   1 SRFAR--LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    94 TESDVQEAMSRLYAALATSARLRAEVSNKPL-VFPDEL-----NKFPELIESETALYNTRR------------------- 148
Cdd:TIGR01843  79 VEADAAELESQVLRLEAEVARLRAEADSQAAiEFPDDLlsaedPAVPELIKGQQSLFESRKstlraqlelilaqikqlea 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   149 --DGLNKATTGLTQGISLVNRELAMTQPLVKQGAASSVEVLRLQR---------------------QANELENKLSDVRT 205
Cdd:TIGR01843 159 elAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELEReraeaqgelgrleaelevlkrQIDELQLERQQIEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   206 QYYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVTTVGGVIAPGGKLMTIVPLDEQLLIEAKISP 285
Cdd:TIGR01843 239 TFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   286 RDVAFIHPGQKSLVKITAYDYSIYGGLPGEVAVISPDTVQDEVRRDVyYYRVYIRTFSNHLENKsKQQFPIFPGMVATVD 365
Cdd:TIGR01843 319 KDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGP-YYRVRISIDQNTLGIG-PKGLELSPGMPVTAD 396
                         410       420
                  ....*....|....*....|....*..
gi 15829798   366 IRTGKKSVLDYLLKPFNKA-QEALRER 391
Cdd:TIGR01843 397 IKTGERTVIEYLLKPITDSvQEALRER 423
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
25-369 1.12e-55

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 186.02  E-value: 1.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  25 VTAVMLLCFLGWAWYFQL---DEVTTGSGTVEpsGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEA 101
Cdd:COG1566  11 ALVLLLLALGLALWAAGRngpDEPVTADGRVE--ARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 102 MSRLYAALATSARLRAEVSNkplvfpdelnkfPELIESETALYNTRRDGLNKAttgltqgislvNRELAMTQPLVKQGAA 181
Cdd:COG1566  89 EAQLAAAEAQLARLEAELGA------------EAEIAAAEAQLAAAQAQLDLA-----------QRELERYQALYKKGAV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 182 SSVEVLRLQRQANELENKLSDVRTQY-----YVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVtT 256
Cdd:COG1566 146 SQQELDEARAALDAAQAQLEAAQAQLaqaqaGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNV-E 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 257 VGGVIAPGGKLMTIVPLDeQLLIEAKISPRDVAFIHPGQKSLVKITAYDYSIYgglPGEVAVISPDTV-----QDEVRRD 331
Cdd:COG1566 225 PGEVVSAGQPLLTIVPLD-DLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSISPGAGftsppKNATGNV 300
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15829798 332 VYYYRVYIRtfsnhLENksKQQFPIFPGMVATVDIRTG 369
Cdd:COG1566 301 VQRYPVRIR-----LDN--PDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
42-339 6.45e-41

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: 147.18  E-value: 6.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    42 LDEVTTGSGTVEPSGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEAMSRLYAALATSARLRAEVSN 121
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   122 KplvfpDELNKFPELIESETALYNTRRDGLNKATTGLTQGISLVNRELAMTQPLVKQGAASSVEVLRLQRQANELENKLS 201
Cdd:pfam00529  84 L-----QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   202 DVRTQ--------------YYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVTTVGGVIAPGGKL 267
Cdd:pfam00529 159 ATVAQldqiyvqitqsaaeNQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRL 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829798   268 MTIVPlDEQLLIEAKISPRDVAFIHPGQKSLVKITAYDYSIYGGLPGEVAVISPDTVQDEVRRDVYYYRVYI 339
Cdd:pfam00529 239 MFVVP-EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYP 309
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
160-297 1.21e-03

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 40.53  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  160 QGISLVNRELAMTQplVKQGAASSVEvLRLQRQANELENKLSDV---------RTQYYV-----QAREELAKANAEVETQ 225
Cdd:PRK11578  87 QLLGVIDPEQAENQ--IKEVEATLME-LRAQRQQAEAELKLARVtlsrqqrlaKTQAVSqqdldTAATELAVKQAQIGTI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  226 RSVIRGREDSL----TRLNFT---APVRGIVQDIdvTTVGG--VIAP--GGKLMTIVPLDeQLLIEAKISPRDVAFIHPG 294
Cdd:PRK11578 164 DAQIKRNQASLdtakTNLDYTrivAPMAGEVTQI--TTLQGqtVIAAqqAPNILTLADMS-TMLVKAQVSEADVIHLKPG 240

                 ...
gi 15829798  295 QKS 297
Cdd:PRK11578 241 QKA 243
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
67-102 7.09e-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: 7.09e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15829798  67 GILYHLDVKVGDIVEQGQPLAQLnrtktesdvqEAM 102
Cdd:cd06850   8 GTVVKVLVKEGDKVEAGQPLAVL----------EAM 33
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
14-391 4.63e-99

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: 300.77  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    14 PRLPRsaLAVRVTAVMLLCFLGWAWYFQLDEVTTGSGTVEPSGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTK 93
Cdd:TIGR01843   1 SRFAR--LITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    94 TESDVQEAMSRLYAALATSARLRAEVSNKPL-VFPDEL-----NKFPELIESETALYNTRR------------------- 148
Cdd:TIGR01843  79 VEADAAELESQVLRLEAEVARLRAEADSQAAiEFPDDLlsaedPAVPELIKGQQSLFESRKstlraqlelilaqikqlea 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   149 --DGLNKATTGLTQGISLVNRELAMTQPLVKQGAASSVEVLRLQR---------------------QANELENKLSDVRT 205
Cdd:TIGR01843 159 elAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELEReraeaqgelgrleaelevlkrQIDELQLERQQIEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   206 QYYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVTTVGGVIAPGGKLMTIVPLDEQLLIEAKISP 285
Cdd:TIGR01843 239 TFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   286 RDVAFIHPGQKSLVKITAYDYSIYGGLPGEVAVISPDTVQDEVRRDVyYYRVYIRTFSNHLENKsKQQFPIFPGMVATVD 365
Cdd:TIGR01843 319 KDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERGGGP-YYRVRISIDQNTLGIG-PKGLELSPGMPVTAD 396
                         410       420
                  ....*....|....*....|....*..
gi 15829798   366 IRTGKKSVLDYLLKPFNKA-QEALRER 391
Cdd:TIGR01843 397 IKTGERTVIEYLLKPITDSvQEALRER 423
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
25-369 1.12e-55

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 186.02  E-value: 1.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  25 VTAVMLLCFLGWAWYFQL---DEVTTGSGTVEpsGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEA 101
Cdd:COG1566  11 ALVLLLLALGLALWAAGRngpDEPVTADGRVE--ARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 102 MSRLYAALATSARLRAEVSNkplvfpdelnkfPELIESETALYNTRRDGLNKAttgltqgislvNRELAMTQPLVKQGAA 181
Cdd:COG1566  89 EAQLAAAEAQLARLEAELGA------------EAEIAAAEAQLAAAQAQLDLA-----------QRELERYQALYKKGAV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 182 SSVEVLRLQRQANELENKLSDVRTQY-----YVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVtT 256
Cdd:COG1566 146 SQQELDEARAALDAAQAQLEAAQAQLaqaqaGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNV-E 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 257 VGGVIAPGGKLMTIVPLDeQLLIEAKISPRDVAFIHPGQKSLVKITAYDYSIYgglPGEVAVISPDTV-----QDEVRRD 331
Cdd:COG1566 225 PGEVVSAGQPLLTIVPLD-DLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSISPGAGftsppKNATGNV 300
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15829798 332 VYYYRVYIRtfsnhLENksKQQFPIFPGMVATVDIRTG 369
Cdd:COG1566 301 VQRYPVRIR-----LDN--PDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
42-339 6.45e-41

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: 147.18  E-value: 6.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    42 LDEVTTGSGTVEPSGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEAMSRLYAALATSARLRAEVSN 121
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   122 KplvfpDELNKFPELIESETALYNTRRDGLNKATTGLTQGISLVNRELAMTQPLVKQGAASSVEVLRLQRQANELENKLS 201
Cdd:pfam00529  84 L-----QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   202 DVRTQ--------------YYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVTTVGGVIAPGGKL 267
Cdd:pfam00529 159 ATVAQldqiyvqitqsaaeNQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRL 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829798   268 MTIVPlDEQLLIEAKISPRDVAFIHPGQKSLVKITAYDYSIYGGLPGEVAVISPDTVQDEVRRDVYYYRVYI 339
Cdd:pfam00529 239 MFVVP-EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYP 309
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
42-371 1.92e-24

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: 102.33  E-value: 1.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  42 LDEVTTGSGTVEPSgREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEAMSRLYAALATSARLRaevsn 121
Cdd:COG0845   8 VPETVEATGTVEAR-REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK----- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 122 kplvfpdelnkfpeliesetalyntrrdglnkattgltqgislvnRELAMTQPLVKQGAASSVEvlrlqrqanelenkls 201
Cdd:COG0845  82 ---------------------------------------------AELERYKALLKKGAVSQQE---------------- 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 202 dvrtqyYVQAREELAKANAEVETQRSVIRGREDSLTRLNFTAPVRGIVQDIDVtTVGGVIAPGGKLMTIVPLDeQLLIEA 281
Cdd:COG0845 101 ------LDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNV-EPGQLVSAGTPLFTIADLD-PLEVEF 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798 282 KISPRDVAFIHPGQKslVKITAYDYSIYgGLPGEVAVISPdTVQDEVRRdvyyYRVYIRtfsnhLENKskqQFPIFPGMV 361
Cdd:COG0845 173 DVPESDLARLKVGQP--VTVTLDAGPGK-TFEGKVTFIDP-AVDPATRT----VRVRAE-----LPNP---DGLLRPGMF 236
                       330
                ....*....|
gi 15829798 362 ATVDIRTGKK 371
Cdd:COG0845 237 VRVRIVLGER 246
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
242-340 1.23e-11

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: 60.84  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   242 TAPVRGIVQDIDVTtVGGVIAPGGKLMTIVPLDEqLLIEAKISPRDVAFIHPGQKSLVKITAY-DYSIygglPGEVAVIS 320
Cdd:pfam13437   3 RAPVDGVVAELNVE-EGQVVQAGDPLATIVPPDR-LLVEAFVPAADLGSLKKGQKVTLKLDPGsDYTL----EGKVVRIS 76
                          90       100
                  ....*....|....*....|
gi 15829798   321 PDtvqdeVRRDVYYYRVYIR 340
Cdd:pfam13437  77 PT-----VDPDTGVIPVRVS 91
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
47-322 1.22e-09

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: 58.87  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798    47 TGSGTVEPsGREQVVQSLEGGILYHLDVKVGDIVEQGQPLAQLNRTKTESDVQEAMSRLYAAlatsarlraevsnkplvf 126
Cdd:TIGR01730  16 TFPGSLEA-VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAA------------------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   127 pdelnkfpeliesETALYNTRRDglnkattgltqgislVNRelamTQPLVKQGAASSVEVLRLQRQaneLENKLSDVRtq 206
Cdd:TIGR01730  77 -------------EAQLELAQRS---------------FER----AERLVKRNAVSQADLDDAKAA---VEAAQADLE-- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   207 yyvQAREELAKANAEVEtqRSVIRgredsltrlnftAPVRGIVQDIDVtTVGGVIAPGGKLMTIVPLDEqLLIEAKISPR 286
Cdd:TIGR01730 120 ---AAKASLASAQLNLR--YTEIR------------APFDGTIGRRLV-EVGAYVTAGQTLATIVDLDP-LEADFSVPER 180
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15829798   287 DVAFIHPGQKSLVKITAYDYSIYgglPGEVAVISPD 322
Cdd:TIGR01730 181 DLPQLRRGQTLTVELDALPGEEF---KGKLRFIDPR 213
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
209-329 4.10e-07

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: 50.20  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798   209 VQAREE--LAKANAEVETQRSVIRGREDSL--------------------TRLNFTAPVRGIVQDIDVTtVGGVIAPGGK 266
Cdd:pfam16576  57 VAAQQEylLALRSGDALSKSELLRAARQRLrllgmpeaqiaelertgkvqPTVTVYAPISGVVTELNVR-EGMYVQPGDT 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829798   267 LMTIVPLDeQLLIEAKISPRDVAFIHPGQKSLVKITAYDYSIYgglPGEVAVISPdTVQDEVR 329
Cdd:pfam16576 136 LFTIADLS-TVWVEADVPEQDLALVKVGQPAEVTLPALPGKTF---EGKVDYIYP-TLDPKTR 193
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
160-297 1.21e-03

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 40.53  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  160 QGISLVNRELAMTQplVKQGAASSVEvLRLQRQANELENKLSDV---------RTQYYV-----QAREELAKANAEVETQ 225
Cdd:PRK11578  87 QLLGVIDPEQAENQ--IKEVEATLME-LRAQRQQAEAELKLARVtlsrqqrlaKTQAVSqqdldTAATELAVKQAQIGTI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829798  226 RSVIRGREDSL----TRLNFT---APVRGIVQDIdvTTVGG--VIAP--GGKLMTIVPLDeQLLIEAKISPRDVAFIHPG 294
Cdd:PRK11578 164 DAQIKRNQASLdtakTNLDYTrivAPMAGEVTQI--TTLQGqtVIAAqqAPNILTLADMS-TMLVKAQVSEADVIHLKPG 240

                 ...
gi 15829798  295 QKS 297
Cdd:PRK11578 241 QKA 243
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
67-102 7.09e-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: 7.09e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15829798  67 GILYHLDVKVGDIVEQGQPLAQLnrtktesdvqEAM 102
Cdd:cd06850   8 GTVVKVLVKEGDKVEAGQPLAVL----------EAM 33
 
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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