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Conserved domains on  [gi|1889614297|ref|WP_182716914|]
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efflux RND transporter periplasmic adaptor subunit [Pseudoalteromonas sp. SG45-2]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
110-409 1.67e-51

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: 175.52  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 110 SSVYAPGEIKANgyKSYVVSPRTESVIISRHAALGEYVEIGQKLVTLFSE-----------AMAQAQADYLIASTEWQRV 178
Cdd:COG0845    10 ETVEATGTVEAR--REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaalaqaqaQLAAAQAQLELAKAELERY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 179 KKL-GNKTVSESRLLQAETTYNASYGKLIAlglTEKAINGISNkdikAFGQYALTAHREGVVLQDDFIQGQRVDAGDSVM 257
Cdd:COG0845    88 KALlKKGAVSQQELDQAKAALDQAQAALAA---AQAALEQARA----NLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 258 LLADEKQLWVEAKVSPNKKLNLSIDSPAVLKLE---GQSYNAKVIQEAHTIDPVTRTRIIRLGVQNADDNLHSGMFVKVY 334
Cdd:COG0845   161 TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDagpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVR 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614297 335 FQFATKQKVMAVPEEALIRSADGDWtVFVEDHPGEFKAVEVELGRALGDFREII-GLDSGTRIVTKGAFFVASEIA 409
Cdd:COG0845   241 IVLGERENALLVPASAVVRDGGGAY-VFVVDADGKVERRPVTLGRRDGDQVEVLsGLKAGDRVVVSGLQRLRDGAK 315
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
110-409 1.67e-51

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: 175.52  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 110 SSVYAPGEIKANgyKSYVVSPRTESVIISRHAALGEYVEIGQKLVTLFSE-----------AMAQAQADYLIASTEWQRV 178
Cdd:COG0845    10 ETVEATGTVEAR--REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaalaqaqaQLAAAQAQLELAKAELERY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 179 KKL-GNKTVSESRLLQAETTYNASYGKLIAlglTEKAINGISNkdikAFGQYALTAHREGVVLQDDFIQGQRVDAGDSVM 257
Cdd:COG0845    88 KALlKKGAVSQQELDQAKAALDQAQAALAA---AQAALEQARA----NLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 258 LLADEKQLWVEAKVSPNKKLNLSIDSPAVLKLE---GQSYNAKVIQEAHTIDPVTRTRIIRLGVQNADDNLHSGMFVKVY 334
Cdd:COG0845   161 TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDagpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVR 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614297 335 FQFATKQKVMAVPEEALIRSADGDWtVFVEDHPGEFKAVEVELGRALGDFREII-GLDSGTRIVTKGAFFVASEIA 409
Cdd:COG0845   241 IVLGERENALLVPASAVVRDGGGAY-VFVVDADGKVERRPVTLGRRDGDQVEVLsGLKAGDRVVVSGLQRLRDGAK 315
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
110-331 7.89e-29

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: 112.21  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 110 SSVYAPGEIKANGYKSYVVSPRTESVIISRHA-ALGEYVEIGQKLVTLFSEAMAQAQADYLIASTewqrvkklGNKTVSE 188
Cdd:pfam16576   4 RTIRAVGRVAYDERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAQQEYLLALR--------SGDALSK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 189 SRLLQAettynaSYGKLIALGLTEKAINGISnKDIKAFGQYALTAHREGVVLQDDFIQGQRVDAGDSVMLLADEKQLWVE 268
Cdd:pfam16576  76 SELLRA------ARQRLRLLGMPEAQIAELE-RTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVE 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614297 269 AKVsPNKKLNL-SIDSPAVLKLE---GQSYNAKVIQEAHTIDPVTRTRIIRLGVQNADDNLHSGMFV 331
Cdd:pfam16576 149 ADV-PEQDLALvKVGQPAEVTLPalpGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
98-404 1.19e-24

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: 103.16  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297  98 IKVESVKPEYQFSSVYAPGEIKANgyKSYVVSPRTESVIISRHAALGEYVEIGQKLVTL-----------FSEAMAQAQA 166
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKISVREGQKVKKGQVLARLddddyqlalqaALAQLAAAEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 167 DYLIASTEWQRVKKL-GNKTVSESRLLQAETTYNASYGKLIALGLTEKAINgisnkdiKAFGQYALTAHREGVVLQDDFI 245
Cdd:TIGR01730  79 QLELAQRSFERAERLvKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQ-------LNLRYTEIRAPFDGTIGRRLVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 246 QGQRVDAGDSVMLLAD----EKQLWVEAK----VSPNKKLNLSIDSPAvlkleGQSYNAKVIQEAHTIDPVTRTRIIRLG 317
Cdd:TIGR01730 152 VGAYVTAGQTLATIVDldplEADFSVPERdlpqLRRGQTLTVELDALP-----GEEFKGKLRFIDPRVDSGTGTVRVRAT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 318 VQNADDNLHSGMFVKVYFQFATKQKVMAVPEEALIRSADGDwTVFVEDHPGEFKAVEVELGRALGDFREII-GLDSGTRI 396
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGK-YVYVVKNDGKVSKRPVEVGLRNGGYVEIEsGLKAGDQI 305

                  ....*...
gi 1889614297 397 VTKGAFFV 404
Cdd:TIGR01730 306 VTAGVVKL 313
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
86-407 8.91e-09

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 57.18  E-value: 8.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297  86 ITIDPKKMSLANIKVESV-KPEYQFSSVYaPGEIKANGYKSYVVSPRTESVIISRHA-ALGEYVEIGQKLVTLFSEAMAQ 163
Cdd:PRK09783   84 VRIDPTQTQNLGVKTATVtRGPLTFAQTF-PANVSYNEYQYAIVQARAAGFIDKVYPlTVGDKVQKGTPLLDLTIPDWVE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 164 AQADYLIAStewqrvKKLGNKTVSESRLlqaettynasyGKLIALGLTEKAING-ISNKDIKAfgQYALTAHREGVVLQD 242
Cdd:PRK09783  163 AQSEYLLLR------ETGGTATQTEGIL-----------ERLRLAGMPEADIRRlIATRKIQT--RFTLKAPIDGVITAF 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 243 DFIQGQRVDAGDSVMLLADEKQLWVEAKVSP------NKKLNLSIDSPAvlkLEGQSYNAKVIQEAHTIDPVTRTRIIRL 316
Cdd:PRK09783  224 DLRAGMNIAKDNVVAKIQGMDPVWVTAAIPEsiawlvKDASQFTLTVPA---RPDKTFTIRKWTLLPSVDAATRTLQLRL 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 317 GVQNADDNLHSGMfvKVYFQFATK-QKVMAVPEEALIRSADgDWTVFVEDHPGEF--KAVEVeLGRALGDFREIIGLDSG 393
Cdd:PRK09783  301 EVDNADEALKPGM--NAWLQLNTAsEPMLLIPSQALIDTGS-EQRVITVDADGRFvpKRVAV-FQESQGVTAIRSGLAEG 376
                         330
                  ....*....|....
gi 1889614297 394 TRIVTKGAFFVASE 407
Cdd:PRK09783  377 EKVVSSGLFLIDSE 390
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
110-409 1.67e-51

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: 175.52  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 110 SSVYAPGEIKANgyKSYVVSPRTESVIISRHAALGEYVEIGQKLVTLFSE-----------AMAQAQADYLIASTEWQRV 178
Cdd:COG0845    10 ETVEATGTVEAR--REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaalaqaqaQLAAAQAQLELAKAELERY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 179 KKL-GNKTVSESRLLQAETTYNASYGKLIAlglTEKAINGISNkdikAFGQYALTAHREGVVLQDDFIQGQRVDAGDSVM 257
Cdd:COG0845    88 KALlKKGAVSQQELDQAKAALDQAQAALAA---AQAALEQARA----NLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 258 LLADEKQLWVEAKVSPNKKLNLSIDSPAVLKLE---GQSYNAKVIQEAHTIDPVTRTRIIRLGVQNADDNLHSGMFVKVY 334
Cdd:COG0845   161 TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDagpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVR 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614297 335 FQFATKQKVMAVPEEALIRSADGDWtVFVEDHPGEFKAVEVELGRALGDFREII-GLDSGTRIVTKGAFFVASEIA 409
Cdd:COG0845   241 IVLGERENALLVPASAVVRDGGGAY-VFVVDADGKVERRPVTLGRRDGDQVEVLsGLKAGDRVVVSGLQRLRDGAK 315
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
110-331 7.89e-29

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: 112.21  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 110 SSVYAPGEIKANGYKSYVVSPRTESVIISRHA-ALGEYVEIGQKLVTLFSEAMAQAQADYLIASTewqrvkklGNKTVSE 188
Cdd:pfam16576   4 RTIRAVGRVAYDERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAQQEYLLALR--------SGDALSK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 189 SRLLQAettynaSYGKLIALGLTEKAINGISnKDIKAFGQYALTAHREGVVLQDDFIQGQRVDAGDSVMLLADEKQLWVE 268
Cdd:pfam16576  76 SELLRA------ARQRLRLLGMPEAQIAELE-RTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVE 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614297 269 AKVsPNKKLNL-SIDSPAVLKLE---GQSYNAKVIQEAHTIDPVTRTRIIRLGVQNADDNLHSGMFV 331
Cdd:pfam16576 149 ADV-PEQDLALvKVGQPAEVTLPalpGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
98-404 1.19e-24

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: 103.16  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297  98 IKVESVKPEYQFSSVYAPGEIKANgyKSYVVSPRTESVIISRHAALGEYVEIGQKLVTL-----------FSEAMAQAQA 166
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKISVREGQKVKKGQVLARLddddyqlalqaALAQLAAAEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 167 DYLIASTEWQRVKKL-GNKTVSESRLLQAETTYNASYGKLIALGLTEKAINgisnkdiKAFGQYALTAHREGVVLQDDFI 245
Cdd:TIGR01730  79 QLELAQRSFERAERLvKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQ-------LNLRYTEIRAPFDGTIGRRLVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 246 QGQRVDAGDSVMLLAD----EKQLWVEAK----VSPNKKLNLSIDSPAvlkleGQSYNAKVIQEAHTIDPVTRTRIIRLG 317
Cdd:TIGR01730 152 VGAYVTAGQTLATIVDldplEADFSVPERdlpqLRRGQTLTVELDALP-----GEEFKGKLRFIDPRVDSGTGTVRVRAT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 318 VQNADDNLHSGMFVKVYFQFATKQKVMAVPEEALIRSADGDwTVFVEDHPGEFKAVEVELGRALGDFREII-GLDSGTRI 396
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGK-YVYVVKNDGKVSKRPVEVGLRNGGYVEIEsGLKAGDQI 305

                  ....*...
gi 1889614297 397 VTKGAFFV 404
Cdd:TIGR01730 306 VTAGVVKL 313
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
107-336 3.02e-14

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 73.16  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 107 YQFSSVYAPGEIKANGY---KSYVVSPRTESVIISRHAALGEYVEIGQKLVTL----FSEAMAQAQADYL---------- 169
Cdd:COG1566    24 WAAGRNGPDEPVTADGRveaRVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLdptdLQAALAQAEAQLAaaeaqlarle 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 170 ------------------------IASTEWQRVKKLGNK-TVSESRLLQAETTYNASYGKLIALGLT-EKAINGISNKDI 223
Cdd:COG1566   104 aelgaeaeiaaaeaqlaaaqaqldLAQRELERYQALYKKgAVSQQELDEARAALDAAQAQLEAAQAQlAQAQAGLREEEE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 224 KA-------------------FGQYALTAHREGVVLQDDFIQGQRVDAGDSVMLLADEKQLWVEAKVSPNKKLNLSIDSP 284
Cdd:COG1566   184 LAaaqaqvaqaeaalaqaelnLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614297 285 AVLKLE---GQSYNAKV------IQEAHTIDPVTRTRIIRLGV-----QNADDNLHSGMFVKVYFQ 336
Cdd:COG1566   264 VEVRVDaypDRVFEGKVtsispgAGFTSPPKNATGNVVQRYPVrirldNPDPEPLRPGMSATVEID 329
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
86-407 8.91e-09

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 57.18  E-value: 8.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297  86 ITIDPKKMSLANIKVESV-KPEYQFSSVYaPGEIKANGYKSYVVSPRTESVIISRHA-ALGEYVEIGQKLVTLFSEAMAQ 163
Cdd:PRK09783   84 VRIDPTQTQNLGVKTATVtRGPLTFAQTF-PANVSYNEYQYAIVQARAAGFIDKVYPlTVGDKVQKGTPLLDLTIPDWVE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 164 AQADYLIAStewqrvKKLGNKTVSESRLlqaettynasyGKLIALGLTEKAING-ISNKDIKAfgQYALTAHREGVVLQD 242
Cdd:PRK09783  163 AQSEYLLLR------ETGGTATQTEGIL-----------ERLRLAGMPEADIRRlIATRKIQT--RFTLKAPIDGVITAF 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 243 DFIQGQRVDAGDSVMLLADEKQLWVEAKVSP------NKKLNLSIDSPAvlkLEGQSYNAKVIQEAHTIDPVTRTRIIRL 316
Cdd:PRK09783  224 DLRAGMNIAKDNVVAKIQGMDPVWVTAAIPEsiawlvKDASQFTLTVPA---RPDKTFTIRKWTLLPSVDAATRTLQLRL 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 317 GVQNADDNLHSGMfvKVYFQFATK-QKVMAVPEEALIRSADgDWTVFVEDHPGEF--KAVEVeLGRALGDFREIIGLDSG 393
Cdd:PRK09783  301 EVDNADEALKPGM--NAWLQLNTAsEPMLLIPSQALIDTGS-EQRVITVDADGRFvpKRVAV-FQESQGVTAIRSGLAEG 376
                         330
                  ....*....|....
gi 1889614297 394 TRIVTKGAFFVASE 407
Cdd:PRK09783  377 EKVVSSGLFLIDSE 390
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
95-400 1.16e-08

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 56.65  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297  95 LANIKVESVKPEYQFSSVYAPGeiKANGYKSYVVSPRTESVIISRHAALGEYVEIGQKLVTL--------FSEA---MAQ 163
Cdd:PRK15030   37 MPAVGVVTVKTEPLQITTELPG--RTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIdpatyqatYDSAkgdLAK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 164 AQADYLIASTEWQRVKKL-GNKTVSESRLLQA-ETTYNASYGKLIALGLTEKA-INGISNKdikafgqyaLTAHREGVVL 240
Cdd:PRK15030  115 AQAAANIAQLTVNRYQKLlGTQYISKQEYDQAlADAQQANAAVTAAKAAVETArINLAYTK---------VTSPISGRIG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 241 QDDFIQGQRVDAGDSVMLlADEKQL---WVEAKVSPNKKLNLSID-SPAVLKLEGQSYNAKVIQEAH------------- 303
Cdd:PRK15030  186 KSNVTEGALVQNGQATAL-ATVQQLdpiYVDVTQSSNDFLRLKQElANGTLKQENGKAKVSLITSDGikfpqdgtlefsd 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 304 -TIDPVTRTRIIRLGVQNADDNLHSGMFVKVYFQFATKQKVMAVPEEALIRSADGDWTVFVEDHPGEFKAVEVELGRALG 382
Cdd:PRK15030  265 vTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIG 344
                         330
                  ....*....|....*....
gi 1889614297 383 DFREII-GLDSGTRIVTKG 400
Cdd:PRK15030  345 DKWLVTeGLKAGDRVVISG 363
PRK09859 PRK09859
multidrug transporter subunit MdtE;
164-400 1.46e-08

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 56.26  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 164 AQADYLIASTEWQRVKklGNKTVSESRLLQAetTYNASYGKLIAlgltekAINGISNKDIKAFGQYaLTAHRegvvlQDD 243
Cdd:PRK09859  135 SRQDYDTARTQLNEAE--ANVTVAKAAVEQA--TINLQYANVTS------PITGVSGKSSVTVGAL-VTANQ-----ADS 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 244 FIQGQRVDAGDSVMLLADEKQLWVEAKVSPNKKLNLSIDSPAVLKLE-GQSY--NAKVIQEAHTIDPVTRTRIIRLGVQN 320
Cdd:PRK09859  199 LVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLEnGKRYsqTGTLKFSDPTVDETTGSVTLRAIFPN 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 321 ADDNLHSGMFVKVYFQFATKQKVMAVPEEALIRSADGDWTVFVEDHPGEFKAVEVELGRALGD-FREIIGLDSGTRIVTK 399
Cdd:PRK09859  279 PNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDqWVVTSGLQAGDRVIVS 358

                  .
gi 1889614297 400 G 400
Cdd:PRK09859  359 G 359
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
231-328 1.82e-07

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: 48.90  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 231 LTAHREGVVLQDDFIQGQRVDAGDSVMLLADEKQLWVEAKVSPNKKLNLSIDSPAVLKLEGQS---YNAKVIQEAHTIDP 307
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSdytLEGKVVRISPTVDP 81
                          90       100
                  ....*....|....*....|...
gi 1889614297 308 VTRTR--IIRLGVQNADDNLHSG 328
Cdd:pfam13437  82 DTGVIpvRVSIENPKTPIPLLPG 104
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
305-410 9.81e-07

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 50.56  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 305 IDPVTRTRIIRLGVQNADDNLHSGMFVKVYFQFATKQKVMAVPEEALIRSADGDwTVFVEDHPGEFKAVEVELGRALG-D 383
Cdd:PRK09578  266 VDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSA-SVKVVGQNGKVRDVEVEADQMSGrD 344
                          90       100
                  ....*....|....*....|....*...
gi 1889614297 384 FREIIGLDSGTR-IVTKGAFFVASEIAK 410
Cdd:PRK09578  345 WIVTRGLAGGERvIVDNAAQFAPGTAVK 372
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
159-329 3.41e-06

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: 48.57  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 159 EAMAQAQADYLIASTEWQRVKKLGNKT-VSESRLLQAETTYN---ASYGKLIA-LGLTEKAINGISNKDIKAF------- 226
Cdd:pfam00529 110 AAVKAAQAQLAQAQIDLARRRVLAPIGgISRESLVTAGALVAqaqANLLATVAqLDQIYVQITQSAAENQAEVrselsga 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614297 227 ------------------GQYALTAHREGVVLQ-DDFIQGQRVDAGDSVMLLADEKQLWVEAKVSPNKKLNLSIDSPAVL 287
Cdd:pfam00529 190 qlqiaeaeaelklakldlERTEIRAPVDGTVAFlSVTVDGGTVSAGLRLMFVVPEDNLLVPGMFVETQLDQVRVGQPVLI 269
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1889614297 288 KLEGQSYNA--KVIQEAHTIDPVTRTRIIRLGVQNADD-NLHSGM 329
Cdd:pfam00529 270 PFDAFPQTKtgRFTGVVVGISPDTGPVRVVVDKAQGPYyPLRIGL 314
 
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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