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Conserved domains on  [gi|520881392|ref|WP_020312670|]
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HlyD family secretion protein [Pseudomonas syringae]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10559 super family cl32535
p-hydroxybenzoic acid efflux pump subunit AaeA;
27-285 2.54e-69

p-hydroxybenzoic acid efflux pump subunit AaeA;


The actual alignment was detected with superfamily member PRK10559:

Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 217.30  E-value: 2.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  27 RMVMYYMYAPWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARR 106
Cdd:PRK10559  27 RAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 107 ENKRNRGLG-NLVAREQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVV 185
Cdd:PRK10559 107 EAGRRNRLGvQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 186 DSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIEDRDRSSGSNLLPNVNPAFSWVRLAQRIPVRIA 265
Cdd:PRK10559 187 KQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIR 266

                        250       260
                 ....*....|....*....|
gi 520881392 266 FDEVPGNfRMIAGRTATVSI 285
Cdd:PRK10559 267 LDNQQGN-LYPAGTTATVVI 285
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
27-285 2.54e-69

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 217.30  E-value: 2.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  27 RMVMYYMYAPWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARR 106
Cdd:PRK10559  27 RAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 107 ENKRNRGLG-NLVAREQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVV 185
Cdd:PRK10559 107 EAGRRNRLGvQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 186 DSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIEDRDRSSGSNLLPNVNPAFSWVRLAQRIPVRIA 265
Cdd:PRK10559 187 KQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIR 266

                        250       260
                 ....*....|....*....|
gi 520881392 266 FDEVPGNfRMIAGRTATVSI 285
Cdd:PRK10559 267 LDNQQGN-LYPAGTTATVVI 285
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
26-285 7.37e-53

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 175.62  E-value: 7.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  26 WRMVMYYMYAPWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQA------------- 92
Cdd:COG1566   24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAqlaaaeaqlarle 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  93 --------------TVAERQETWEQARRENKRNRGL--GNLVAREQLEESQSREARALSALGES---------------- 140
Cdd:COG1566  104 aelgaeaeiaaaeaQLAAAQAQLDLAQRELERYQALykKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeee 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 141 -----------RVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQG 209
Cdd:COG1566  184 laaaqaqvaqaEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520881392 210 VDIRVIG-DNARLTGHVVSIVAGIEDRDrssgsnllPNVNPAFswvRLAQRIPVRIAFDEVPGNfRMIAGRTATVSI 285
Cdd:COG1566  264 VEVRVDAyPDRVFEGKVTSISPGAGFTS--------PPKNATG---NVVQRYPVRIRLDNPDPE-PLRPGMSATVEI 328
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 46-214 5.72e-27

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 107.02  E-value: 5.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   46 DIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNLVAREQL 123
Cdd:TIGR01730  25 DEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvkRNAVSQADL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  124 EESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDG 203
Cdd:TIGR01730 105 DDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQ 184

                         170
                  ....*....|.
gi 520881392  204 IHVGQGVDIRV 214
Cdd:TIGR01730 185 LRRGQTLTVEL 195
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 36-234 4.72e-24

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: 99.42  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   36 PWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVA-------------ERQETWE 102
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAkaqaqvarlqaelDRLQALE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  103 Q-------------------------------------ARRENKRNRGL---------GNLVA----------------- 119
Cdd:pfam00529  89 SelaisrqdydgataqlraaqaavkaaqaqlaqaqidlARRRVLAPIGGisreslvtaGALVAqaqanllatvaqldqiy 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  120 -------REQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPR-DHEFVTAGRPVLSVVDSASFH 191
Cdd:pfam00529 169 vqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLL 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 520881392  192 IDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIED 234
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISP 291
 
Name Accession Description Interval E-value
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
27-285 2.54e-69

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 217.30  E-value: 2.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  27 RMVMYYMYAPWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARR 106
Cdd:PRK10559  27 RAWVFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 107 ENKRNRGLG-NLVAREQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVV 185
Cdd:PRK10559 107 EAGRRNRLGvQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 186 DSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIEDRDRSSGSNLLPNVNPAFSWVRLAQRIPVRIA 265
Cdd:PRK10559 187 KQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIR 266

                        250       260
                 ....*....|....*....|
gi 520881392 266 FDEVPGNfRMIAGRTATVSI 285
Cdd:PRK10559 267 LDNQQGN-LYPAGTTATVVI 285
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
26-285 7.37e-53

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 175.62  E-value: 7.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  26 WRMVMYYMYAPWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQA------------- 92
Cdd:COG1566   24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAqlaaaeaqlarle 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  93 --------------TVAERQETWEQARRENKRNRGL--GNLVAREQLEESQSREARALSALGES---------------- 140
Cdd:COG1566  104 aelgaeaeiaaaeaQLAAAQAQLDLAQRELERYQALykKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeee 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 141 -----------RVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQG 209
Cdd:COG1566  184 laaaqaqvaqaEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520881392 210 VDIRVIG-DNARLTGHVVSIVAGIEDRDrssgsnllPNVNPAFswvRLAQRIPVRIAFDEVPGNfRMIAGRTATVSI 285
Cdd:COG1566  264 VEVRVDAyPDRVFEGKVTSISPGAGFTS--------PPKNATG---NVVQRYPVRIRLDNPDPE-PLRPGMSATVEI 328
PRK10476 PRK10476
multidrug transporter subunit MdtN;
35-285 3.04e-41

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 145.55  E-value: 3.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  35 APWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQA---------------------- 92
Cdd:PRK10476  36 APSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQAdlaladaqimttqrsvdaersn 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  93 ------TVAERQETWEQARRENKRNRGLG--NLVAREQ--------------LEESQSREARALSALG----------ES 140
Cdd:PRK10476 116 aasaneQVERARANAKLATRTLERLEPLLakGYVSAQQvdqartaqrdaevsLNQALLQAQAAAAAVGgvdalvaqraAR 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 141 RVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNAR 220
Cdd:PRK10476 196 EAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGR 275

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520881392 221 -LTGHVVSIVAGIEDRDRSSGSNLLPNVNPAFSWVRLAQRIPVRIAFDEVPGN-FRMiaGRTATVSI 285
Cdd:PRK10476 276 pFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDKPDPElFRI--GASAVVEL 340
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 41-291 1.93e-39

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 140.46  E-value: 1.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  41 GHIRAD-IVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNL 117
Cdd:COG0845   16 GTVEARrEVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALlkKGA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 118 VAREQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFE 197
Cdd:COG0845   96 VSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 198 ETKLDGIHVGQGVDIRV-IGDNARLTGHVVSIvagiedrdrssgsnlLPNVNPAfswvrlAQRIPVRIAFDEVPGNFRmi 276
Cdd:COG0845  176 ESDLARLKVGQPVTVTLdAGPGKTFEGKVTFI---------------DPAVDPA------TRTVRVRAELPNPDGLLR-- 232

                        250
                 ....*....|....*
gi 520881392 277 AGRTATVSIIDDTQE 291
Cdd:COG0845  233 PGMFVRVRIVLGERE 247
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 46-214 5.72e-27

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 107.02  E-value: 5.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   46 DIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNLVAREQL 123
Cdd:TIGR01730  25 DEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLvkRNAVSQADL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  124 EESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDG 203
Cdd:TIGR01730 105 DDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQ 184

                         170
                  ....*....|.
gi 520881392  204 IHVGQGVDIRV 214
Cdd:TIGR01730 185 LRRGQTLTVEL 195
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
38-268 9.47e-26

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 105.16  E-value: 9.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  38 TRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLAL---------------------RQAQATVAE 96
Cdd:PRK15136  52 TDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFekaktalansvrqthqlminsKQYQANIEL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  97 RQETWEQARRENKRNRGLG--NLVAREQLEESQSREARALSALGESRVAVDAAQ-------------------------L 149
Cdd:PRK15136 132 QKTALAQAQSDLNRRVPLGnaNLIGREELQHARDAVASAQAQLDVAIQQYNANQamilntpledqpavqqaatevrnawL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392 150 NLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQGVDI--RVIGDNARLTGHVVS 227
Cdd:PRK15136 212 ALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATItsDIYGDDVVYTGKVVG 291

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 520881392 228 IvagiedrDRSSGS--NLLPNVNPAFSWVRLAQRIPVRIAFDE 268
Cdd:PRK15136 292 L-------DMGTGSafSLLPAQNATGNWIKVVQRLPVRIELDA 327
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 36-234 4.72e-24

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: 99.42  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   36 PWTRDGHIRADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVA-------------ERQETWE 102
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAkaqaqvarlqaelDRLQALE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  103 Q-------------------------------------ARRENKRNRGL---------GNLVA----------------- 119
Cdd:pfam00529  89 SelaisrqdydgataqlraaqaavkaaqaqlaqaqidlARRRVLAPIGGisreslvtaGALVAqaqanllatvaqldqiy 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  120 -------REQLEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPR-DHEFVTAGRPVLSVVDSASFH 191
Cdd:pfam00529 169 vqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLL 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 520881392  192 IDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIED 234
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISP 291
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
45-162 1.02e-14

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 73.67  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  45 ADIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGLG--NLVAREQ 122
Cdd:PRK11556  85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAktNLVSRQE 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 520881392 123 LEESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDG 162
Cdd:PRK11556 165 LDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISG 204
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
48-95 1.32e-14

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 66.70  E-value: 1.32e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 520881392   48 VQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVA 95
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 155-237 1.75e-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: 54.29  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  155 VIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNAR-LTGHVVSIVAGIE 233
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYtLEGKVVRISPTVD 80


                  ....
gi 520881392  234 DRDR 237
Cdd:pfam13437  81 PDTG 84
PRK09859 PRK09859
multidrug transporter subunit MdtE;
46-162 1.10e-08

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 55.49  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  46 DIVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNLVAREQL 123
Cdd:PRK09859  60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLlkTNYVSRQDY 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520881392 124 EESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDG 162
Cdd:PRK09859 140 DTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITG 178
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 46-213 2.20e-08

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 54.58  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  46 DI--VQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATV--------------------------AER 97
Cdd:PRK03598  40 DIrtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVsvaqaqldlmlagyrdeeiaqaraavKQA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  98 QETWEQARRENKRNRGL-----------------------GNLVAREQLeeSQSRE-------ARALSALGESRVAVDAA 147
Cdd:PRK03598 120 QAAYDYAQNFYNRQQGLwksrtisandlenarssrdqaqaTLKSAQDKL--SQYREgnrpqdiAQAKASLAQAQAALAQA 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520881392 148 QLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQGVDIR 213
Cdd:PRK03598 198 ELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLY 263
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 41-228 5.75e-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: 49.04  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   41 GHIRAD---IVQIAPDVSGLIQKVEV-TDNQPVHKGQVLFTIDKDrfrlALRQAQatvaerqETWEQARReNKRNRGLGN 116
Cdd:pfam16576  10 GRVAYDerrLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSP----ELVAAQ-------QEYLLALR-SGDALSKSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  117 LV--AREQLEESQSREArALSALGESRVAvdaaqlnLDRSVIRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDG 194
Cdd:pfam16576  78 LLraARQRLRLLGMPEA-QIAELERTGKV-------QPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEA 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 520881392  195 YFEETKLDGIHVGQGVDIRVIG-DNARLTGHVVSI 228
Cdd:pfam16576 150 DVPEQDLALVKVGQPAEVTLPAlPGKTFEGKVDYI 184
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
47-179 8.28e-07

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 49.71  E-value: 8.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  47 IVQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNLVAREQLE 124
Cdd:PRK15030  65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLlgTQYISKQEYD 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 520881392 125 ESQSREARALSALGESRVAVDAAQLNLDRSVIRSPVDGYLNDRAPRDHEFVTAGR 179
Cdd:PRK15030 145 QALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQ 199
8a0102 TIGR00999
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ...
 67-254 1.04e-06

Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]


Pssm-ID: 273386 [Multi-domain]  Cd Length: 265  Bit Score: 48.97  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   67 QPVHKGQVLFTIDKDRFRLA---LRQAQATVAERQETWEqaRRENKRNRGLGN----LVAREQLEESQSREARALSALGE 139
Cdd:TIGR00999   2 DPVKKGQVLAVVDSPELAKMaaeLKVAQKRVELARKTYE--REKKLFEQGVIPrqefESAEYALEEAQAEVQAAKSELRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  140 SRVAVDAAQLNLdrsviRSPVDGYLNDRAPRDHEFVTAGRPVLSVVDSASFHIDGYFEETKLDGIHVGQGVDIRVIGDnA 219
Cdd:TIGR00999  80 AREAKDGSYVEV-----RSPFDGYITQKSVTLGDYVAPQAELFRVADLGAVWVEAEVPAKDVSRIRKGSKATVLLENG-R 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 520881392  220 RLTGHVVSIVAGIEDRDRSSGSNLLPNvNPAFSWV 254
Cdd:TIGR00999 154 PLPARVDYVGPEVDGSSRTAKVRVLIK-NENLTLK 187
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
54-178 2.30e-06

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 48.25  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  54 VSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENKRNRGL--GNLVAREQLEESQSREA 131
Cdd:PRK09578  70 VAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLvrDRAVSERDYTEAVADER 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 520881392 132 RALSALGESRVAVDAAQLNLDRSVIRSPVDGylndRAPRdhEFVTAG 178
Cdd:PRK09578 150 QAKAAVASAKAELARAQLQLDYATVTAPIDG----RARR--ALVTEG 190
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 86-286 5.19e-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: 47.31  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392   86 ALRQAQATVAERQETWEQARREnkrnrglgnlvAREQLEESQSRearalsaLGESRVAVDAAQLNLDRSVIRSPVDGYLN 165
Cdd:TIGR01843 222 LKRQIDELQLERQQIEQTFREE-----------VLEELTEAQAR-------LAELRERLNKARDRLQRLIIRSPVDGTVQ 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  166 drAPRDHE---FVTAGRPVLSVV-DSASFHIDGYFEETKLDGIHVGQGVDIRVIGDNARLTGHVVSIVAGIeDRDRSSGS 241
Cdd:TIGR01843 284 --SLKVHTvggVVQPGETLMEIVpEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSI-SPDTFTDE 360

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 520881392  242 NLLPNVnpafswvrlaqrIPVRIAFDEV-----PGNFRMIAGRTATVSII 286
Cdd:TIGR01843 361 RGGGPY------------YRVRISIDQNtlgigPKGLELSPGMPVTADIK 398
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 48-162 9.92e-05

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 43.22  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520881392  48 VQIAPDVSGLIQKVEVTDNQPVHKGQVLFTIDKDRFRLALRQAQATVAERQETWEQARRENK-------RNRGLGNL--V 118
Cdd:PRK11578  62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKlarvtlsRQQRLAKTqaV 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520881392 119 AREQLEES-------QSREARALSALGESRVAVDAAQLNLDRSVIRSPVDG 162
Cdd:PRK11578 142 SQQDLDTAatelavkQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAG 192
 
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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