NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1738963702|emb|VAT82038|]
View 

secretion protein HlyD [Klebsiella pneumoniae]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
31-403 5.53e-41

Multidrug resistance efflux pump EmrA [Defense mechanisms];


:

Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 148.27  E-value: 5.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  31 WLIVILssCFLIALISTLILCTFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISRNTTNGN 110
Cdd:COG1566     9 LLALVL--LLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 111 VSLAQTAVINEKIINAESIItklirnkdetlnaldtqlnTIKKSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITK 190
Cdd:COG1566    87 QAEAQLAAAEAQLARLEAEL-------------------GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 191 DQYNYQHSLYFQQQSAYQSLVSQKMQLESQITQftsdkvtkaadfDNQISNQQNQINDYKNQLVESDAK-GNVIIKATTD 269
Cdd:COG1566   148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLRE------------EEELAAAQAQVAQAEAALAQAELNlARTTIRAPVD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 270 GRIESLAVTKGQMVDNGSSLAQIKPTGNVeyYLILWLPNNSIPYVKPGDTINIRYDAFPADKfgqFPGEVISISSMPASR 349
Cdd:COG1566   216 GVVTNLNVEPGEVVSAGQPLLTIVPLDDL--WVEAYVPETDLGRVKPGQPVEVRVDAYPDRV---FEGKVTSISPGAGFT 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738963702 350 QemseyTNVNNGTNQQelALYKTIVKIKqksfsyNGKTLYLSNGLKAEAVVFLE 403
Cdd:COG1566   291 S-----PPKNATGNVV--QRYPVRIRLD------NPDPEPLRPGMSATVEIDTE 331
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
31-403 5.53e-41

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 148.27  E-value: 5.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  31 WLIVILssCFLIALISTLILCTFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISRNTTNGN 110
Cdd:COG1566     9 LLALVL--LLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 111 VSLAQTAVINEKIINAESIItklirnkdetlnaldtqlnTIKKSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITK 190
Cdd:COG1566    87 QAEAQLAAAEAQLARLEAEL-------------------GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 191 DQYNYQHSLYFQQQSAYQSLVSQKMQLESQITQftsdkvtkaadfDNQISNQQNQINDYKNQLVESDAK-GNVIIKATTD 269
Cdd:COG1566   148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLRE------------EEELAAAQAQVAQAEAALAQAELNlARTTIRAPVD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 270 GRIESLAVTKGQMVDNGSSLAQIKPTGNVeyYLILWLPNNSIPYVKPGDTINIRYDAFPADKfgqFPGEVISISSMPASR 349
Cdd:COG1566   216 GVVTNLNVEPGEVVSAGQPLLTIVPLDDL--WVEAYVPETDLGRVKPGQPVEVRVDAYPDRV---FEGKVTSISPGAGFT 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738963702 350 QemseyTNVNNGTNQQelALYKTIVKIKqksfsyNGKTLYLSNGLKAEAVVFLE 403
Cdd:COG1566   291 S-----PPKNATGNVV--QRYPVRIRLD------NPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
52-402 7.49e-40

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: 145.26  E-value: 7.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  52 TFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISRNTTNGNVSLAQ--TAVINEKIINAESi 129
Cdd:pfam00529   3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQlaKAQAQVARLQAEL- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 130 itKLIRNKDETLNALDTQLNTIKKSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITKDQYNYQHSLYFQQQSAYQS 209
Cdd:pfam00529  82 --DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 210 LVSQKMQLESQITQFTSDKvtkAADFDNQISNQQNQINDYKNQLVESDAKG-NVIIKATTDGRIESLAV-TKGQMVDNGS 287
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAEN---QAEVRSELSGAQLQIAEAEAELKLAKLDLeRTEIRAPVDGTVAFLSVtVDGGTVSAGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 288 SLAQIKPTGNveYYLILWLPNNSIPYVKPGDTINIRYDAFPADKFGQFPGEVISISSMPASRQemseytnvnngtnqqel 367
Cdd:pfam00529 237 RLMFVVPEDN--LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVR----------------- 297
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1738963702 368 alyktiVKIKQKSFSYngktLYLSNGLKAEAVVFL 402
Cdd:pfam00529 298 ------VVVDKAQGPY----YPLRIGLSAGALVRL 322
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
29-420 1.22e-24

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: 105.09  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  29 PAWLIVILSSCFLIAListLILCTFTQrIDV----RGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISR 104
Cdd:TIGR01843   3 FARLITWLIAGLVVIF---FLWAYFAP-LDVvataTGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 105 -----NTTNGNVsLAQTAVINEKIINAES--------------------IITKLIRNKDETLNALDTQLN----TIKKSL 155
Cdd:TIGR01843  79 veadaAELESQV-LRLEAEVARLRAEADSqaaiefpddllsaedpavpeLIKGQQSLFESRKSTLRAQLElilaQIKQLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 156 SETTSMLANTQAGLNKM---HQNLSSYDKYLKEGLITKDQYNYQHSLYFQQQSAYQSLVSQKMQLESQITQFTSDKVTKA 232
Cdd:TIGR01843 158 AELAGLQAQLQALRQQLeviSEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 233 ADFDNQISNQ----QNQINDYKNQLVE-SDAKGNVIIKATTDGRIESLAV-TKGQMVDNGSSLAQIKPTGN---VEYYLi 303
Cdd:TIGR01843 238 QTFREEVLEElteaQARLAELRERLNKaRDRLQRLIIRSPVDGTVQSLKVhTVGGVVQPGETLMEIVPEDDpleIEAKL- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 304 lwlPNNSIPYVKPGDTINIRYDAFPADKFGQFPGEVISISsmPASRQEmseytnvnngtNQQELALYKTIVKIKQKSFSY 383
Cdd:TIGR01843 317 ---SPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSIS--PDTFTD-----------ERGGGPYYRVRISIDQNTLGI 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1738963702 384 NGKTLYLSNGLKAEAVVFLEERPLYMWMFTPFYKISQ 420
Cdd:TIGR01843 381 GPKGLELSPGMPVTADIKTGERTVIEYLLKPITDSVQ 417
PRK09859 PRK09859
multidrug transporter subunit MdtE;
65-178 5.72e-04

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 42.01  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  65 TLPHSVNVFAPQ-QGFVLNQYVKVGDIVKKGQKLYEID-----ISRNTTNGNVSLAQTAVINEKI-INAESIITKLIRNK 137
Cdd:PRK09859   56 TVPYEVAEIRPQvGGIIIKRNFIEGDKVNQGDSLYQIDpaplqAELNSAKGSLAKALSTASNARItFNRQASLLKTNYVS 135
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1738963702 138 DETLNALDTQLNTIKKSLseTTSMLANTQAGLNKMHQNLSS 178
Cdd:PRK09859  136 RQDYDTARTQLNEAEANV--TVAKAAVEQATINLQYANVTS 174
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
31-403 5.53e-41

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 148.27  E-value: 5.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  31 WLIVILssCFLIALISTLILCTFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISRNTTNGN 110
Cdd:COG1566     9 LLALVL--LLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 111 VSLAQTAVINEKIINAESIItklirnkdetlnaldtqlnTIKKSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITK 190
Cdd:COG1566    87 QAEAQLAAAEAQLARLEAEL-------------------GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 191 DQYNYQHSLYFQQQSAYQSLVSQKMQLESQITQftsdkvtkaadfDNQISNQQNQINDYKNQLVESDAK-GNVIIKATTD 269
Cdd:COG1566   148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLRE------------EEELAAAQAQVAQAEAALAQAELNlARTTIRAPVD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 270 GRIESLAVTKGQMVDNGSSLAQIKPTGNVeyYLILWLPNNSIPYVKPGDTINIRYDAFPADKfgqFPGEVISISSMPASR 349
Cdd:COG1566   216 GVVTNLNVEPGEVVSAGQPLLTIVPLDDL--WVEAYVPETDLGRVKPGQPVEVRVDAYPDRV---FEGKVTSISPGAGFT 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738963702 350 QemseyTNVNNGTNQQelALYKTIVKIKqksfsyNGKTLYLSNGLKAEAVVFLE 403
Cdd:COG1566   291 S-----PPKNATGNVV--QRYPVRIRLD------NPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
52-402 7.49e-40

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: 145.26  E-value: 7.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  52 TFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISRNTTNGNVSLAQ--TAVINEKIINAESi 129
Cdd:pfam00529   3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQlaKAQAQVARLQAEL- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 130 itKLIRNKDETLNALDTQLNTIKKSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITKDQYNYQHSLYFQQQSAYQS 209
Cdd:pfam00529  82 --DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 210 LVSQKMQLESQITQFTSDKvtkAADFDNQISNQQNQINDYKNQLVESDAKG-NVIIKATTDGRIESLAV-TKGQMVDNGS 287
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAEN---QAEVRSELSGAQLQIAEAEAELKLAKLDLeRTEIRAPVDGTVAFLSVtVDGGTVSAGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 288 SLAQIKPTGNveYYLILWLPNNSIPYVKPGDTINIRYDAFPADKFGQFPGEVISISSMPASRQemseytnvnngtnqqel 367
Cdd:pfam00529 237 RLMFVVPEDN--LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVR----------------- 297
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1738963702 368 alyktiVKIKQKSFSYngktLYLSNGLKAEAVVFL 402
Cdd:pfam00529 298 ------VVVDKAQGPY----YPLRIGLSAGALVRL 322
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
29-420 1.22e-24

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: 105.09  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  29 PAWLIVILSSCFLIAListLILCTFTQrIDV----RGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISR 104
Cdd:TIGR01843   3 FARLITWLIAGLVVIF---FLWAYFAP-LDVvataTGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 105 -----NTTNGNVsLAQTAVINEKIINAES--------------------IITKLIRNKDETLNALDTQLN----TIKKSL 155
Cdd:TIGR01843  79 veadaAELESQV-LRLEAEVARLRAEADSqaaiefpddllsaedpavpeLIKGQQSLFESRKSTLRAQLElilaQIKQLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 156 SETTSMLANTQAGLNKM---HQNLSSYDKYLKEGLITKDQYNYQHSLYFQQQSAYQSLVSQKMQLESQITQFTSDKVTKA 232
Cdd:TIGR01843 158 AELAGLQAQLQALRQQLeviSEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 233 ADFDNQISNQ----QNQINDYKNQLVE-SDAKGNVIIKATTDGRIESLAV-TKGQMVDNGSSLAQIKPTGN---VEYYLi 303
Cdd:TIGR01843 238 QTFREEVLEElteaQARLAELRERLNKaRDRLQRLIIRSPVDGTVQSLKVhTVGGVVQPGETLMEIVPEDDpleIEAKL- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 304 lwlPNNSIPYVKPGDTINIRYDAFPADKFGQFPGEVISISsmPASRQEmseytnvnngtNQQELALYKTIVKIKQKSFSY 383
Cdd:TIGR01843 317 ---SPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSIS--PDTFTD-----------ERGGGPYYRVRISIDQNTLGI 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1738963702 384 NGKTLYLSNGLKAEAVVFLEERPLYMWMFTPFYKISQ 420
Cdd:TIGR01843 381 GPKGLELSPGMPVTADIKTGERTVIEYLLKPITDSVQ 417
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
52-349 2.84e-17

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: 82.30  E-value: 2.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  52 TFTQRIDVRGEViTLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDisrnttngnvslaqtavinekiinaesiit 131
Cdd:COG0845     7 DVPETVEATGTV-EARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLD------------------------------ 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 132 klirnkDETLNAldtqlntikkSLSETTSMLANTQAGLNKMHQNLSSYDKYLKEGLITKDQYNYQHSLYFQQQSAYQSlv 211
Cdd:COG0845    56 ------PPDLQA----------ALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAA-- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 212 sqkmqlesqitqftsdkvTKAadfdnQISNQQNQINDYKnqlvesdakgnviIKATTDGRIESLAVTKGQMVDNGSSLAQ 291
Cdd:COG0845   118 ------------------AQA-----ALEQARANLAYTT-------------IRAPFDGVVGERNVEPGQLVSAGTPLFT 161
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 292 IKPTGNVeyYLILWLPNNSIPYVKPGDTINIRYDAFPADkfgQFPGEVISISSM--PASR 349
Cdd:COG0845   162 IADLDPL--EVEFDVPESDLARLKVGQPVTVTLDAGPGK---TFEGKVTFIDPAvdPATR 216
NHLM_micro_HlyD TIGR03794
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the ...
30-352 1.52e-16

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: 81.04  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  30 AWLIVILSSCFLIALISTLILCTFTQRIDVRGEVITLPHSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEIDISR---NT 106
Cdd:TIGR03794  19 SWLALAALGVIVVAALAWGIFGSIPITVSGNGILILSSGVDTIQSPGSGVVIDLDVEVGDQVKKGQVVARLFQPElreRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 107 TNGNVSLAQTAVINEKIIN---------------AESIITKLIRNKDETLNALDTQLNTIKKSLSETTSMLANTQAGLNK 171
Cdd:TIGR03794  99 QESYQKLTQLQEQLEEVRNytgrlkegrerhfqkSKEALEETIGRLREELAALSREVGKQRGLLSRGLATFKRDRILQQQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 172 MHQNLSSYDKYLKEGLItkdqynYQhslyFQQQSAYQSLVSQKMQLESQITQFTSDKVTKAADFDNQISNQQNQINDYKN 251
Cdd:TIGR03794 179 WREEQAKYDAADKARAI------YA----LQTKADERNLETVLQSLSQADFQLAGVAQQELETVEARIKEARYEIEELEN 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 252 QLvesdaKGNVIIKATTDGRIESLAVTKGQMVDNGSSLAQIKPTGNVEYYL--ILWLPNNSIPYVKPGDTINIRYDAFPA 329
Cdd:TIGR03794 249 KL-----NLNTRIVSQHSGRVIELNYTPGQLVAAGAPLASLEVEDQTDEGLegVAYFPVAEGKKIRPGMSVQITPSTVKA 323
                         330       340
                  ....*....|....*....|...
gi 1738963702 330 DKFGQFPGEVISISSMPASRQEM 352
Cdd:TIGR03794 324 ERDGYIRGTVTSVSEYPATKEAM 346
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
264-349 8.36e-09

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: 52.75  E-value: 8.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 264 IKATTDGRIESLAVTKGQMVDNGSSLAQIKPTGNVEYYliLWLPNNSIPYVKPGDTINIRYDAFPADkfgQFPGEVISIS 343
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVE--AFVPAADLGSLKKGQKVTLKLDPGSDY---TLEGKVVRIS 76

                  ....*.
gi 1738963702 344 SMPASR 349
Cdd:pfam13437  77 PTVDPD 82
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
74-346 6.05e-07

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: 50.78  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  74 APQQ-GFVLNQYVKVGDIVKKGQKLYEIDisrnttngnvslaqtavinekiinaesiitklirnkDETLNAldtQLNTIK 152
Cdd:TIGR01730  30 AAEVaGKITKISVREGQKVKKGQVLARLD------------------------------------DDDYQL---ALQAAL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 153 KSLSETTSMLANTQAGLNKmhqnlssYDKYLKEGLITKdqynyqhslyfqqqsayQSLVSQKMQLESQITQFTSDKVTKA 232
Cdd:TIGR01730  71 AQLAAAEAQLELAQRSFER-------AERLVKRNAVSQ-----------------ADLDDAKAAVEAAQADLEAAKASLA 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 233 ADfdnqisnqQNQINDYKnqlvesdakgnviIKATTDGRIESLAVTKGQMVDNGSSLAQIkpTGNVEYYLILWLPNNSIP 312
Cdd:TIGR01730 127 SA--------QLNLRYTE-------------IRAPFDGTIGRRLVEVGAYVTAGQTLATI--VDLDPLEADFSVPERDLP 183
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1738963702 313 YVKPGDTINIRYDAFPADkfgQFPGEVISISSMP 346
Cdd:TIGR01730 184 QLRRGQTLTVELDALPGE---EFKGKLRFIDPRV 214
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
251-349 1.25e-05

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: 45.96  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702 251 NQLVES-DAKGNVIIKATTDGRIESLAVTKGQMVDNGSSLAQIKPTGNVeyylilWL----PNNSIPYVKPGDTINIRYD 325
Cdd:pfam16576  97 AELERTgKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTV------WVeadvPEQDLALVKVGQPAEVTLP 170
                          90       100
                  ....*....|....*....|....*.
gi 1738963702 326 AFPaDKfgQFPGEVISISSM--PASR 349
Cdd:pfam16576 171 ALP-GK--TFEGKVDYIYPTldPKTR 193
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
68-101 7.91e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 40.12  E-value: 7.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1738963702  68 HSVNVFAPQQGFVLNQYVKVGDIVKKGQKLYEID 101
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLD 34
PRK09859 PRK09859
multidrug transporter subunit MdtE;
65-178 5.72e-04

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 42.01  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963702  65 TLPHSVNVFAPQ-QGFVLNQYVKVGDIVKKGQKLYEID-----ISRNTTNGNVSLAQTAVINEKI-INAESIITKLIRNK 137
Cdd:PRK09859   56 TVPYEVAEIRPQvGGIIIKRNFIEGDKVNQGDSLYQIDpaplqAELNSAKGSLAKALSTASNARItFNRQASLLKTNYVS 135
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1738963702 138 DETLNALDTQLNTIKKSLseTTSMLANTQAGLNKMHQNLSS 178
Cdd:PRK09859  136 RQDYDTARTQLNEAEANV--TVAKAAVEQATINLQYANVTS 174
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH