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Conserved domains on  [gi|1437768077|emb|STO77286|]
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Type I secretion system membrane fusion protein PrsE [Grimontia hollisae]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 32-466 5.42e-124

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


The actual alignment was detected with superfamily member TIGR01843:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 423  Bit Score: 367.41  E-value: 5.42e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  32 PKSTRILLWVIALFIIVTAVWAAFAELDKVTVGQGKVIPSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDTMFR 111
Cdd:TIGR01843   1 SRFARLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 112 SDFRERVQELTSLQGDAVKLQSLVESvvvnpetgvenwqEAVTIQRNELVFTPEFqeEHRAVVARQRAEYRDKLNNLQNQ 191
Cdd:TIGR01843  81 ADAAELESQVLRLEAEVARLRAEADS-------------QAAIEFPDDLLSAEDP--AVPELIKGQQSLFESRKSTLRAQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 192 LSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLPSITSS 271
Cdd:TIGR01843 146 LELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQ 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 272 LQEAVFKHIDVALKFRAEQQERLSDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNTVGGVIQPGMDLVEIVP 351
Cdd:TIGR01843 226 IDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVP 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 352 SEDNLLIEAKIAPQDIAFLRPGLEAIVKFSAYDFTVYGGLTGILETISADTIQDEE-GNSFYLVKIRTESNNLGEGEE-L 429
Cdd:TIGR01843 306 EDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERgGGPYYRVRISIDQNTLGIGPKgL 385

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1437768077 430 PIIPGMTASTDIITGKRSVLDYLLKPILQAQKSALRE 466
Cdd:TIGR01843 386 ELSPGMPVTADIKTGERTVIEYLLKPITDSVQEALRE 422
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 32-466 5.42e-124

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: 367.41  E-value: 5.42e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  32 PKSTRILLWVIALFIIVTAVWAAFAELDKVTVGQGKVIPSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDTMFR 111
Cdd:TIGR01843   1 SRFARLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 112 SDFRERVQELTSLQGDAVKLQSLVESvvvnpetgvenwqEAVTIQRNELVFTPEFqeEHRAVVARQRAEYRDKLNNLQNQ 191
Cdd:TIGR01843  81 ADAAELESQVLRLEAEVARLRAEADS-------------QAAIEFPDDLLSAEDP--AVPELIKGQQSLFESRKSTLRAQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 192 LSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLPSITSS 271
Cdd:TIGR01843 146 LELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQ 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 272 LQEAVFKHIDVALKFRAEQQERLSDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNTVGGVIQPGMDLVEIVP 351
Cdd:TIGR01843 226 IDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVP 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 352 SEDNLLIEAKIAPQDIAFLRPGLEAIVKFSAYDFTVYGGLTGILETISADTIQDEE-GNSFYLVKIRTESNNLGEGEE-L 429
Cdd:TIGR01843 306 EDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERgGGPYYRVRISIDQNTLGIGPKgL 385

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1437768077 430 PIIPGMTASTDIITGKRSVLDYLLKPILQAQKSALRE 466
Cdd:TIGR01843 386 ELSPGMPVTADIKTGERTVIEYLLKPITDSVQEALRE 422
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
30-444 1.94e-46

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 163.68  E-value: 1.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  30 STPKSTRILLWVIALFIIVTAVWAAFAEL-DKVTVGQGKVipSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDT 108
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAAGRNGpDEPVTADGRV--EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 109 mfrsDFRERVQELtslqgdavklqslvesvvvnpetgvenwqeavtiqrnelvftpefqeehRAVVARQRAEYRDklnnl 188
Cdd:COG1566    80 ----DLQAALAQA-------------------------------------------------EAQLAAAEAQLAR----- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 189 qnqlsvtAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLpsi 268
Cdd:COG1566   102 -------LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQL--- 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 269 tsslqeavfkhidVALKFRAEQQERLSDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNtVGGVIQPGMDLVE 348
Cdd:COG1566   172 -------------AQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE-PGEVVSAGQPLLT 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 349 IVPSeDNLLIEAKIAPQDIAFLRPGLEAIVKFSAYDFTVYgglTGILETISADTI-----QDEEGN--SFYLVKIRTEsn 421
Cdd:COG1566   238 IVPL-DDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSISPGAGftsppKNATGNvvQRYPVRIRLD-- 311

                         410       420
                  ....*....|....*....|...
gi 1437768077 422 nlgEGEELPIIPGMTASTDIITG 444
Cdd:COG1566   312 ---NPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 55-406 4.91e-35

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: 132.93  E-value: 4.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  55 FAELDKVTVGQGKVIPSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDTMFRSDFRERVQELTSLQGDAVKLQSL 134
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 135 VEsvvvnpetgvenwqeavtiqrnelvftpefqeehravvaRQRAeyrdklnnLQNQLSVTAQQIRQKEQELIEVEARVQ 214
Cdd:pfam00529  81 LD---------------------------------------RLQA--------LESELAISRQDYDGATAQLRAAQAAVK 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 215 NLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLPSITSSLQEAVFkhidvalKFRAEQQERL 294
Cdd:pfam00529 114 AAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-------ENQAEVRSEL 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 295 SDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNTVGGVIQPGMDLVEIVPsEDNLLIEAKIAPQDIAFLRPGL 374
Cdd:pfam00529 187 SGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVP-EDNLLVPGMFVETQLDQVRVGQ 265

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1437768077 375 EAIVKFSAYDFTVYGGLTGILETISADTIQDE 406
Cdd:pfam00529 266 PVLIPFDAFPQTKTGRFTGVVVGISPDTGPVR 297
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 57-107 2.33e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.19  E-value: 2.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1437768077  57 ELDKVTVGqgkvIPSSQlqvvqnleGGLIKKLLVHEGDTVEEGQQLLLIDD 107
Cdd:PRK11855   39 ETDKATME----IPSPA--------AGVVKEIKVKVGDTVSVGGLLAVIEA 77
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 32-466 5.42e-124

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: 367.41  E-value: 5.42e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  32 PKSTRILLWVIALFIIVTAVWAAFAELDKVTVGQGKVIPSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDTMFR 111
Cdd:TIGR01843   1 SRFARLITWLIAGLVVIFFLWAYFAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 112 SDFRERVQELTSLQGDAVKLQSLVESvvvnpetgvenwqEAVTIQRNELVFTPEFqeEHRAVVARQRAEYRDKLNNLQNQ 191
Cdd:TIGR01843  81 ADAAELESQVLRLEAEVARLRAEADS-------------QAAIEFPDDLLSAEDP--AVPELIKGQQSLFESRKSTLRAQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 192 LSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLPSITSS 271
Cdd:TIGR01843 146 LELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQ 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 272 LQEAVFKHIDVALKFRAEQQERLSDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNTVGGVIQPGMDLVEIVP 351
Cdd:TIGR01843 226 IDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVP 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 352 SEDNLLIEAKIAPQDIAFLRPGLEAIVKFSAYDFTVYGGLTGILETISADTIQDEE-GNSFYLVKIRTESNNLGEGEE-L 429
Cdd:TIGR01843 306 EDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSISPDTFTDERgGGPYYRVRISIDQNTLGIGPKgL 385

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1437768077 430 PIIPGMTASTDIITGKRSVLDYLLKPILQAQKSALRE 466
Cdd:TIGR01843 386 ELSPGMPVTADIKTGERTVIEYLLKPITDSVQEALRE 422
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
30-444 1.94e-46

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 163.68  E-value: 1.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  30 STPKSTRILLWVIALFIIVTAVWAAFAEL-DKVTVGQGKVipSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDT 108
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAAGRNGpDEPVTADGRV--EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 109 mfrsDFRERVQELtslqgdavklqslvesvvvnpetgvenwqeavtiqrnelvftpefqeehRAVVARQRAEYRDklnnl 188
Cdd:COG1566    80 ----DLQAALAQA-------------------------------------------------EAQLAAAEAQLAR----- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 189 qnqlsvtAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLpsi 268
Cdd:COG1566   102 -------LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQL--- 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 269 tsslqeavfkhidVALKFRAEQQERLSDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNtVGGVIQPGMDLVE 348
Cdd:COG1566   172 -------------AQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE-PGEVVSAGQPLLT 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 349 IVPSeDNLLIEAKIAPQDIAFLRPGLEAIVKFSAYDFTVYgglTGILETISADTI-----QDEEGN--SFYLVKIRTEsn 421
Cdd:COG1566   238 IVPL-DDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF---EGKVTSISPGAGftsppKNATGNvvQRYPVRIRLD-- 311

                         410       420
                  ....*....|....*....|...
gi 1437768077 422 nlgEGEELPIIPGMTASTDIITG 444
Cdd:COG1566   312 ---NPDPEPLRPGMSATVEIDTE 331
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 55-406 4.91e-35

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: 132.93  E-value: 4.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  55 FAELDKVTVGQGKVIPSSQLQVVQNLEGGLIKKLLVHEGDTVEEGQQLLLIDDTMFRSDFRERVQELTSLQGDAVKLQSL 134
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 135 VEsvvvnpetgvenwqeavtiqrnelvftpefqeehravvaRQRAeyrdklnnLQNQLSVTAQQIRQKEQELIEVEARVQ 214
Cdd:pfam00529  81 LD---------------------------------------RLQA--------LESELAISRQDYDGATAQLRAAQAAVK 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 215 NLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLPSITSSLQEAVFkhidvalKFRAEQQERL 294
Cdd:pfam00529 114 AAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-------ENQAEVRSEL 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 295 SDVEDKLLAMTETRVTLADRVERTVVVSPVNGTIKKLHVNTVGGVIQPGMDLVEIVPsEDNLLIEAKIAPQDIAFLRPGL 374
Cdd:pfam00529 187 SGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVP-EDNLLVPGMFVETQLDQVRVGQ 265

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1437768077 375 EAIVKFSAYDFTVYGGLTGILETISADTIQDE 406
Cdd:pfam00529 266 PVLIPFDAFPQTKTGRFTGVVVGISPDTGPVR 297
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 200-446 1.06e-11

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: 65.73  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 200 RQKEQELIEVEARVQNLRQSYRFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRELSSAELSLpsitsslqeavfkh 279
Cdd:COG0845    57 PDLQAALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAAL-------------- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 280 idvalkfrAEQQERLsdvedkllamtetrvtladrvERTVVVSPVNGTIKKLHVnTVGGVIQPGMDLVEIVpSEDNLLIE 359
Cdd:COG0845   123 --------EQARANL---------------------AYTTIRAPFDGVVGERNV-EPGQLVSAGTPLFTIA-DLDPLEVE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 360 AKIAPQDIAFLRPGLEAIVKFSAYDFTVYgglTGILETISAdTIQDEEGNsfylVKIRTESNNlgegEELPIIPGMTAST 439
Cdd:COG0845   172 FDVPESDLARLKVGQPVTVTLDAGPGKTF---EGKVTFIDP-AVDPATRT----VRVRAELPN----PDGLLRPGMFVRV 239


                  ....*..
gi 1437768077 440 DIITGKR 446
Cdd:COG0845   240 RIVLGER 246
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 319-434 3.69e-11

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 59.68  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 319 VVVSPVNGTIKKLHVNtVGGVIQPGMDLVEIVPsEDNLLIEAKIAPQDIAFLRPGLEAIVKFSAY-DFTVygglTGILET 397
Cdd:pfam13437   1 TIRAPVDGVVAELNVE-EGQVVQAGDPLATIVP-PDRLLVEAFVPAADLGSLKKGQKVTLKLDPGsDYTL----EGKVVR 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1437768077 398 ISADTiqdEEGNSFYLVKIRTEsnnlGEGEELPIIPG 434
Cdd:pfam13437  75 ISPTV---DPDTGVIPVRVSIE----NPKTPIPLLPG 104
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 288-402 6.22e-07

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 50.20  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 288 AEQQERLSDVEDKLLA-MTETRvtladRVERTV-VVSPVNGTIKKLHVNtVGGVIQPGMDLVEIVpSEDNLLIEAKIAPQ 365
Cdd:pfam16576  82 ARQRLRLLGMPEAQIAeLERTG-----KVQPTVtVYAPISGVVTELNVR-EGMYVQPGDTLFTIA-DLSTVWVEADVPEQ 154

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1437768077 366 DIAFLRPGLEAIVKFSAY-DFTVYGGLTGILETISADT 402
Cdd:pfam16576 155 DLALVKVGQPAEVTLPALpGKTFEGKVDYIYPTLDPKT 192
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
171-265 2.20e-04

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 43.49  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 171 RAVVARQRAEYRDKLNNLQNQLSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYsitkplaDEGVVPQIDLLKLQRQ 250
Cdd:COG1538   264 KAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAEEALELARARY-------RAGLASLLDVLDAQRE 336

                          90
                  ....*....|....*
gi 1437768077 251 VNDTQRELSSAELSL 265
Cdd:COG1538   337 LLQAQLNLIQARYDY 351
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-317 1.35e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  115 RERVQELTSLQGDAVKLQSLVESVVV-NPETGVENWQEAVTIQRNELvftpEFQEEHRAVVARQRAEYRDKLNNLQNQ-- 191
Cdd:COG4913    258 RELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEELRAEL----ARLEAELERLEARLDALREELDELEAQir 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077  192 ------LSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYsitkPLADEgvvpqiDLLKLQRQVNDTQRELSSAElsl 265
Cdd:COG4913    334 gnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPL----PASAE------EFAALRAEAAALLEALEEEL--- 400

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1437768077  266 psitSSLQEAVFKHIDValkfRAEQQERLSDVEDKLLAMTETRVTLADRVER 317
Cdd:COG4913    401 ----EALEEALAEAEAA----LRDLRRELRELEAEIASLERRKSNIPARLLA 444
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 57-107 2.33e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.19  E-value: 2.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1437768077  57 ELDKVTVGqgkvIPSSQlqvvqnleGGLIKKLLVHEGDTVEEGQQLLLIDD 107
Cdd:PRK11855   39 ETDKATME----IPSPA--------AGVVKEIKVKVGDTVSVGGLLAVIEA 77
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
 109-274 2.70e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 39.96  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 109 MFRSDFRERVQELT---------SLQGDAVKLQ-SLVESVVVNPETGVENWQEA--VTIQRNELVFTPEFQEEHRAVVAR 176
Cdd:pfam17060  65 IYKESFSEMFNGLVgnnfktvinKIFEDCDGIPaSFISALELKEDVKSSPRSEAdsLGTPIKVDLLRNLKPQESPETPRR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 177 QRAEYRD---KLNNLQNQLSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYSITKplaDEGVVPQidllklqrqvND 253
Cdd:pfam17060 145 INRKYKSlelRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYK---QHHEHGG----------NN 211

                         170       180
                  ....*....|....*....|.
gi 1437768077 254 TQRELSSAELSLPSITSSLQE 274
Cdd:pfam17060 212 SIKTATKHEFIISELKRKLQE 232
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
316-390 2.75e-03

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 40.06  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437768077 316 ERTVVVSPVNGTIKKLHVNtVGGVIQPGMDLVEIVPSeDNLLIEAKIAPQDIAFLRPGLEAIVKFSAY-DFTVYGG 390
Cdd:PRK15136  214 QRTKIVSPMTGYVSRRSVQ-VGAQISPTTPLMAVVPA-TNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTG 287
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 167-331 3.03e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 167 QEEHRAVVARQRAEYRDKLNNLQNQLSVTAQQIRQKEQELIEVEARVQNLRQSYRFAHEEYS-ITKPLADEGVVPQIDLL 245
Cdd:COG4942    46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRALYRLGRQPPLALL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 246 KLQRQVNDTQRELSSAELSLPSITSSLQEAVFKHIDVALKfRAEQQERLSDVEDKLLAMTETRVTL-ADRVERTVVVSPV 324
Cdd:COG4942   126 LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALeALKAERQKLLARL 204


                  ....*..
gi 1437768077 325 NGTIKKL 331
Cdd:COG4942   205 EKELAEL 211
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 102-276 3.38e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.09  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 102 LLLIDDTMFRSDFRERVQELTSLQGDAVKLQSLVESVVVNpetgVENWQEAVTIQRNELvftpefqEEHRAVVARQRAEY 181
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ----IENLEEKEMNLRDEL-------ESVREEFIQKGDEV 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437768077 182 RDKLNNLQNQLSVTAQQIRQKEQELIEVEARVQNLRQSY----RFAHEEYSITKPLADEGVVPQIDLLKLQRQVNDTQRE 257
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIenknKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644

                         170
                  ....*....|....*....
gi 1437768077 258 LSSAELSLPSITSSLQEAV 276
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEI 663
 
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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