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Conserved domains on  [gi|851963178|ref|WP_048233783|]
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MULTISPECIES: HlyD family secretion protein [Serratia]

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

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List of domain hits

Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-298 5.42e-30

Multidrug resistance efflux pump EmrA [Defense mechanisms];


:

Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 115.53  E-value: 5.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  51 VDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLPG----------LK 120
Cdd:COG1566   41 VEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAeaeiaaaeaqLA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 121 QKATRLKMAAQAGAAQMQLS----------DEAYEAVQQAKTAVTVAQAQANLAERRL-----------------AKLVE 173
Cdd:COG1566  121 AAQAQLDLAQRELERYQALYkkgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLreeeelaaaqaqvaqaeAALAQ 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 174 HGAQLD---LRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSERKDlpTA 250
Cdd:COG1566  201 AELNLArttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF--EG 278
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 851963178 251 HVIRISSTFVLSQLQENAQQSPRRVVECILAFDSEPSTL--VGQNVVVSF 298
Cdd:COG1566  279 KVTSISPGAGFTSPPKNATGNVVQRYPVRIRLDNPDPEPlrPGMSATVEI 328
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-298 5.42e-30

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 115.53  E-value: 5.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  51 VDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLPG----------LK 120
Cdd:COG1566   41 VEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAeaeiaaaeaqLA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 121 QKATRLKMAAQAGAAQMQLS----------DEAYEAVQQAKTAVTVAQAQANLAERRL-----------------AKLVE 173
Cdd:COG1566  121 AAQAQLDLAQRELERYQALYkkgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLreeeelaaaqaqvaqaeAALAQ 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 174 HGAQLD---LRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSERKDlpTA 250
Cdd:COG1566  201 AELNLArttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF--EG 278
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 851963178 251 HVIRISSTFVLSQLQENAQQSPRRVVECILAFDSEPSTL--VGQNVVVSF 298
Cdd:COG1566  279 KVTSISPGAGFTSPPKNATGNVVQRYPVRIRLDNPDPEPlrPGMSATVEI 328
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
56-239 6.03e-17

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: 79.67  E-value: 6.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   56 VALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLpglkQKATRLkmaaqagAA 135
Cdd:TIGR01730  27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSF----ERAERL-------VK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  136 QMQLSDEAYEavqQAKTAVTVAQAQANLAERRLAKLVEHGAQLDLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFI 215
Cdd:TIGR01730  96 RNAVSQADLD---DAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLE 172
                         170       180
                  ....*....|....*....|....
gi 851963178  216 IRAELNESYLAGVKVGMKAKVQID 239
Cdd:TIGR01730 173 ADFSVPERDLPQLRRGQTLTVELD 196
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
47-239 4.55e-14

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: 71.30  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   47 GKVDVDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLPGLKQKATRL 126
Cdd:pfam00529  12 GRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  127 KMAAQAGAAQMQLSDEAYEAVQQAKTAVT-----------------------------VAQAQANL-------------- 163
Cdd:pfam00529  92 AISRQDYDGATAQLRAAQAAVKAAQAQLAqaqidlarrrvlapiggisreslvtagalVAQAQANLlatvaqldqiyvqi 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  164 ------------------------AERRLAKLVEHGAQLDLRAPFAGSIVKLNAQ-EGAFISSGQPVILFLPNKPFIIRA 218
Cdd:pfam00529 172 tqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLLVPG 251
                         250       260
                  ....*....|....*....|.
gi 851963178  219 ELNESYLAGVKVGMKAKVQID 239
Cdd:pfam00529 252 MFVETQLDQVRVGQPVLIPFD 272
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
55-236 5.87e-10

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 58.98  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  55 IVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYyaDKRVAESEIAVAVAQlqgigeQLPGLKQKATRLKMAAQAGA 134
Cdd:PRK10559  47 VVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRY--QKALAEAEADVAYYQ------VLAQEKRREAGRRNRLGVQA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 135 AQMQLSDEAYEAVQQAKTAVTVAQAQANLAERRLAKLVehgaqldLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPF 214
Cdd:PRK10559 119 MSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTV-------IRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSF 191
                        170       180
                 ....*....|....*....|..
gi 851963178 215 IIRAELNESYLAGVKVGMKAKV 236
Cdd:PRK10559 192 YVLAYMEETKLEGVRPGYRAEI 213
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-298 5.42e-30

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 115.53  E-value: 5.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  51 VDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLPG----------LK 120
Cdd:COG1566   41 VEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAeaeiaaaeaqLA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 121 QKATRLKMAAQAGAAQMQLS----------DEAYEAVQQAKTAVTVAQAQANLAERRL-----------------AKLVE 173
Cdd:COG1566  121 AAQAQLDLAQRELERYQALYkkgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLreeeelaaaqaqvaqaeAALAQ 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 174 HGAQLD---LRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSERKDlpTA 250
Cdd:COG1566  201 AELNLArttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF--EG 278
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 851963178 251 HVIRISSTFVLSQLQENAQQSPRRVVECILAFDSEPSTL--VGQNVVVSF 298
Cdd:COG1566  279 KVTSISPGAGFTSPPKNATGNVVQRYPVRIRLDNPDPEPlrPGMSATVEI 328
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
56-259 1.02e-27

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: 109.26  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  56 VALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGigeqlpgLKQKATRLKMAAQAGAA 135
Cdd:COG0845   24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLEL-------AKAELERYKALLKKGAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 136 QMQLSDEAYEAVQQAKTAVTVAQAQANLAERRLAKLVehgaqldLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFI 215
Cdd:COG0845   97 SQQELDQAKAALDQAQAALAAAQAALEQARANLAYTT-------IRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLE 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 851963178 216 IRAELNESYLAGVKVGMKAKVQIDNDSERKDlpTAHVIRISSTF 259
Cdd:COG0845  170 VEFDVPESDLARLKVGQPVTVTLDAGPGKTF--EGKVTFIDPAV 211
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
56-239 6.03e-17

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: 79.67  E-value: 6.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   56 VALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLpglkQKATRLkmaaqagAA 135
Cdd:TIGR01730  27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSF----ERAERL-------VK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  136 QMQLSDEAYEavqQAKTAVTVAQAQANLAERRLAKLVEHGAQLDLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFI 215
Cdd:TIGR01730  96 RNAVSQADLD---DAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLE 172
                         170       180
                  ....*....|....*....|....
gi 851963178  216 IRAELNESYLAGVKVGMKAKVQID 239
Cdd:TIGR01730 173 ADFSVPERDLPQLRRGQTLTVELD 196
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
47-239 4.55e-14

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: 71.30  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   47 GKVDVDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQGIGEQLPGLKQKATRL 126
Cdd:pfam00529  12 GRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  127 KMAAQAGAAQMQLSDEAYEAVQQAKTAVT-----------------------------VAQAQANL-------------- 163
Cdd:pfam00529  92 AISRQDYDGATAQLRAAQAAVKAAQAQLAqaqidlarrrvlapiggisreslvtagalVAQAQANLlatvaqldqiyvqi 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  164 ------------------------AERRLAKLVEHGAQLDLRAPFAGSIVKLNAQ-EGAFISSGQPVILFLPNKPFIIRA 218
Cdd:pfam00529 172 tqsaaenqaevrselsgaqlqiaeAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLLVPG 251
                         250       260
                  ....*....|....*....|.
gi 851963178  219 ELNESYLAGVKVGMKAKVQID 239
Cdd:pfam00529 252 MFVETQLDQVRVGQPVLIPFD 272
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
55-236 5.87e-10

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 58.98  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  55 IVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYyaDKRVAESEIAVAVAQlqgigeQLPGLKQKATRLKMAAQAGA 134
Cdd:PRK10559  47 VVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRY--QKALAEAEADVAYYQ------VLAQEKRREAGRRNRLGVQA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 135 AQMQLSDEAYEAVQQAKTAVTVAQAQANLAERRLAKLVehgaqldLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPF 214
Cdd:PRK10559 119 MSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTV-------IRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSF 191
                        170       180
                 ....*....|....*....|..
gi 851963178 215 IIRAELNESYLAGVKVGMKAKV 236
Cdd:PRK10559 192 YVLAYMEETKLEGVRPGYRAEI 213
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
180-259 9.77e-10

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: 55.06  E-value: 9.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  180 LRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSERKdlPTAHVIRISSTF 259
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYT--LEGKVVRISPTV 79
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
51-244 4.04e-07

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 50.73  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  51 VDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQL---------QGIGEQLPGLKQ 121
Cdd:PRK03598  39 VDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLdlmlagyrdEEIAQARAAVKQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 122 KATRLKMAAQAGAAQMQL-----------------SDEAYEAVQQAKTAVT-----------------VAQAQANLAERR 167
Cdd:PRK03598 119 AQAAYDYAQNFYNRQQGLwksrtisandlenarssRDQAQATLKSAQDKLSqyregnrpqdiaqakasLAQAQAALAQAE 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851963178 168 LAKlvehgAQLDLRAPFAGSIVKLNAQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSER 244
Cdd:PRK03598 199 LNL-----QDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDK 270
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
42-256 1.56e-06

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: 49.24  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   42 VAIARGKVDVDGGIVALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVA-------------- 107
Cdd:TIGR01843  30 VATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAevarlraeadsqaa 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  108 -----------------------------------QLQGIGEQLPGLKQKATRLKMAAQAGAAQMQLSDEAYEA------ 146
Cdd:TIGR01843 110 iefpddllsaedpavpelikgqqslfesrkstlraQLELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEArrklke 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  147 ---------------------------------------------------VQQAKTAVTVAQAQANLAERRLAKLVEHG 175
Cdd:TIGR01843 190 kglvsrlellelereraeaqgelgrleaelevlkrqidelqlerqqieqtfREEVLEELTEAQARLAELRERLNKARDRL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  176 AQLDLRAPFAGSIVKL-NAQEGAFISSGQPVILFLP-NKPFIIRAELNESYLAGVKVGMKAKVQIDN-DSERKDLPTAHV 252
Cdd:TIGR01843 270 QRLIIRSPVDGTVQSLkVHTVGGVVQPGETLMEIVPeDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAfPYRRYGILNGKV 349

                  ....
gi 851963178  253 IRIS 256
Cdd:TIGR01843 350 KSIS 353
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
45-176 5.57e-06

ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.


Pssm-ID: 213754 [Multi-domain]  Cd Length: 327  Bit Score: 47.13  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   45 ARGKVDVDGGIVALSFPSEGV---VDKVLVTEGQAVQKGQILMQQDHRlyyaDKRVAESEIA---VAVAQLQgigeqlpg 118
Cdd:TIGR02971   3 ALGRLEPEGEVVAVAAPSSGGtdrIKKLLVAEGDRVQAGQVLAELDSR----PERTAELDVArtqLDEAKAR-------- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851963178  119 LKQKATRLKMAAQAGAAQMQLSDEAYEAVQQAKTAVTVAQAQANLAER---RLAKLVEHGA 176
Cdd:TIGR02971  71 LAQVRAGAKKGEIAAQRAARAAAKLFKDVAAQQATLNRLEAELETAQRevdRYRSLFRDGA 131
PRK10476 PRK10476
multidrug transporter subunit MdtN;
71-244 2.16e-05

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 45.40  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  71 VTEGQAVQKGQILMQQDHRLYYADKRVAESEIAVAVAQLQG-----IGEQLPG------LKQKATRLKMAAQAGAAQMQL 139
Cdd:PRK10476  64 VTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTtqrsvDAERSNAasaneqVERARANAKLATRTLERLEPL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178 140 SDEAY---EAVQQAKTA-----VTVAQA--QANLAER-------RLAKLVEHGAQLDL----------RAPFAGSIVKLN 192
Cdd:PRK10476 144 LAKGYvsaQQVDQARTAqrdaeVSLNQAllQAQAAAAavggvdaLVAQRAAREAALAIaelhledttvRAPFDGRVVGLK 223
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851963178 193 AQEGAFISSGQPVILFLPNKPFIIRAELNESYLAGVKVGMKAKVQIDNDSER 244
Cdd:PRK10476 224 VSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGR 275
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
47-239 6.07e-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: 43.26  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178   47 GKVDVDG-GIVALSFPSEGVVDKVLV-TEGQAVQKGQILMqqdhRLYYADKRVAESEIAVAVAQLQGIGEQlpGLKQKAT 124
Cdd:pfam16576  10 GRVAYDErRLAHVHARVEGWIEKLYVnATGDPVKKGQPLA----ELYSPELVAAQQEYLLALRSGDALSKS--ELLRAAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  125 -RLKMAAqagaaqmqLSDEAYEAVQQAKTAVTVaqaqanlaerrlaklvehgaqLDLRAPFAGSIVKLNAQEGAFISSGQ 203
Cdd:pfam16576  84 qRLRLLG--------MPEAQIAELERTGKVQPT---------------------VTVYAPISGVVTELNVREGMYVQPGD 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 851963178  204 PVilflpnkpFIIR--------AELNESYLAGVKVGMKAKVQID 239
Cdd:pfam16576 135 TL--------FTIAdlstvwveADVPEQDLALVKVGQPAEVTLP 170
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
56-103 8.70e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 39.35  E-value: 8.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 851963178   56 VALSFPSEGVVDKVLVTEGQAVQKGQILMQQDHRLYYADKRVAESEIA 103
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
20-207 4.70e-04

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 41.24  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  20 LSGCDDKPVK------PVATAPTQAVVPVAIArgkVDVDGGIVALSFPS-----EGVVDKVLVTEGQAVQKGQILMQQDH 88
Cdd:PRK15030  22 LTGCDDKQAQqggqqmPAVGVVTVKTEPLQIT---TELPGRTSAYRIAEvrpqvSGIILKRNFKEGSDIEAGVSLYQIDP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851963178  89 RLYYADKRVAESEIAVAVAqlqgiGEQLPGLKQKatRLKMAAQAGAAQMQLSDEAYEAVQQAKTAVTVAQAQANLAERRL 168
Cdd:PRK15030  99 ATYQATYDSAKGDLAKAQA-----AANIAQLTVN--RYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINL 171
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 851963178 169 AklvehgaQLDLRAPFAGSIVKLNAQEGAFISSGQPVIL 207
Cdd:PRK15030 172 A-------YTKVTSPISGRIGKSNVTEGALVQNGQATAL 203
 
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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