NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|486198972|ref|WP_001548143|]
View 

MULTISPECIES: Cu(+)/Ag(+) efflux RND transporter periplasmic adaptor subunit SilB [Enterobacterales]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11484481)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Escherichia coli cation efflux system protein CusB, which is part of a cation efflux system that mediates resistance to copper and silver

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 6-413 0e+00

copper/silver efflux system membrane fusion protein CusB; Provisional


:

Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 836.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972   6 IKYAAIIISSLIAGGLISVTAWQYLNSSQKTVQTEQKApEKKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADESGDK 85
Cdd:PRK09783   1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTSTA-ERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  86 SSGGIRIDPTQVQNLGLKTQKVTRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPE 165
Cdd:PRK09783  80 SSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 166 WVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQ 245
Cdd:PRK09783 160 WVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 246 IQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGMNAYLKL 325
Cdd:PRK09783 240 IQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 326 NTQSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALER 405
Cdd:PRK09783 320 NTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALER 399


                 ....*...
gi 486198972 406 MRHPEKTE 413
Cdd:PRK09783 400 MRSESATH 407
 
Name Accession Description Interval E-value
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 6-413 0e+00

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 836.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972   6 IKYAAIIISSLIAGGLISVTAWQYLNSSQKTVQTEQKApEKKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADESGDK 85
Cdd:PRK09783   1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTSTA-ERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  86 SSGGIRIDPTQVQNLGLKTQKVTRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPE 165
Cdd:PRK09783  80 SSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 166 WVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQ 245
Cdd:PRK09783 160 WVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 246 IQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGMNAYLKL 325
Cdd:PRK09783 240 IQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 326 NTQSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALER 405
Cdd:PRK09783 320 NTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALER 399


                 ....*...
gi 486198972 406 MRHPEKTE 413
Cdd:PRK09783 400 MRSESATH 407
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 111-321 1.22e-80

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: 247.81  E-value: 1.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  111 MLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPEWVEAQSEFLLLSGTGGTPTQ---IK 187
Cdd:pfam16576   1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  188 GVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLK 267
Cdd:pfam16576  81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 486198972  268 DTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGMNA 321
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 106-405 1.34e-54

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: 183.99  E-value: 1.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 106 KVTRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTIGDHVKKGTPLIDITIP----EWVEAQSEfllLSGTGG 181
Cdd:COG0845    2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPdlqaALAQAQAQ---LAAAQA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 182 TPTQIKGVLERLR-LAG---MPEEDIQ------------------RLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISK 239
Cdd:COG0845   76 QLELAKAELERYKaLLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 240 DKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGM 319
Cdd:COG0845  156 GTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 320 NAYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEAN 398
Cdd:COG0845  236 FVRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315


                 ....*..
gi 486198972 399 ITGALER 405
Cdd:COG0845  316 VRVVEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 103-393 3.29e-30

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: 118.96  E-value: 3.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  103 KTQKVTRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTIGDHVKKGTPLIDI-------------TIPEWVEA 169
Cdd:TIGR01730   2 TVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  170 QSEFL---------LLSGTGGTPTQIKGVLERLRLAgmpEEDIQRLRSTRT---IQTRFT-IKAPIDGVITAFDLRTGMN 236
Cdd:TIGR01730  79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAA---QADLEAAKASLAsaqLNLRYTeIRAPFDGTIGRRLVEVGAY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  237 ISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLK 316
Cdd:TIGR01730 156 VTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  317 PGMNAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVlheSQQQSG---IGSGLNEGDTVVVSGLFL 392
Cdd:TIGR01730 236 PGMFGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVK 312


                  .
gi 486198972  393 I 393
Cdd:TIGR01730 313 L 313
 
Name Accession Description Interval E-value
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 6-413 0e+00

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 836.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972   6 IKYAAIIISSLIAGGLISVTAWQYLNSSQKTVQTEQKApEKKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADESGDK 85
Cdd:PRK09783   1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTSTA-ERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  86 SSGGIRIDPTQVQNLGLKTQKVTRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPE 165
Cdd:PRK09783  80 SSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 166 WVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQ 245
Cdd:PRK09783 160 WVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 246 IQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGMNAYLKL 325
Cdd:PRK09783 240 IQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 326 NTQSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALER 405
Cdd:PRK09783 320 NTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALER 399


                 ....*...
gi 486198972 406 MRHPEKTE 413
Cdd:PRK09783 400 MRSESATH 407
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 111-321 1.22e-80

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: 247.81  E-value: 1.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  111 MLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPEWVEAQSEFLLLSGTGGTPTQ---IK 187
Cdd:pfam16576   1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  188 GVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLK 267
Cdd:pfam16576  81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 486198972  268 DTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGMNA 321
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 106-405 1.34e-54

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: 183.99  E-value: 1.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 106 KVTRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTIGDHVKKGTPLIDITIP----EWVEAQSEfllLSGTGG 181
Cdd:COG0845    2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPdlqaALAQAQAQ---LAAAQA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 182 TPTQIKGVLERLR-LAG---MPEEDIQ------------------RLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISK 239
Cdd:COG0845   76 QLELAKAELERYKaLLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 240 DKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLKPGM 319
Cdd:COG0845  156 GTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 320 NAYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEAN 398
Cdd:COG0845  236 FVRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315


                 ....*..
gi 486198972 399 ITGALER 405
Cdd:COG0845  316 VRVVEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 103-393 3.29e-30

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: 118.96  E-value: 3.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  103 KTQKVTRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTIGDHVKKGTPLIDI-------------TIPEWVEA 169
Cdd:TIGR01730   2 TVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  170 QSEFL---------LLSGTGGTPTQIKGVLERLRLAgmpEEDIQRLRSTRT---IQTRFT-IKAPIDGVITAFDLRTGMN 236
Cdd:TIGR01730  79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAA---QADLEAAKASLAsaqLNLRYTeIRAPFDGTIGRRLVEVGAY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  237 ISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVSNKDEFLK 316
Cdd:TIGR01730 156 VTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  317 PGMNAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVlheSQQQSG---IGSGLNEGDTVVVSGLFL 392
Cdd:TIGR01730 236 PGMFGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVK 312


                  .
gi 486198972  393 I 393
Cdd:TIGR01730 313 L 313
HlyD_D4 pfam16572
Long alpha hairpin domain of cation efflux system protein, CusB; HlyD_D4 is the long ...
 158-209 3.15e-19

Long alpha hairpin domain of cation efflux system protein, CusB; HlyD_D4 is the long alpha-hairpin domain in the centre of CusB or HlyD proteins. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. 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. HlyD_D4 is thought to interact with the alpha-helical tunnels of the corresponding outer-membrane channels, ie the periplasmic domain of CusC.


Pssm-ID: 406875 [Multi-domain]  Cd Length: 54  Bit Score: 80.77  E-value: 3.15e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 486198972  158 LIDITIPEWVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPEEDIQRLRST 209
Cdd:pfam16572   1 LLDLLIPEWVAAQEEYLALRRTGDTASLTDGARERLRLAGMPESDIRRLEAS 52
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 112-387 2.47e-14

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 73.61  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  112 LNYSQTIPANVSYNEYQfVIVQARSDGFVEKVYpLTIGDHVKKGTPLIDITIPEWVEA---------------------- 169
Cdd:pfam00529   4 LTKGVEAPGRVVVSGNA-KAVQPQVSGIVTRVL-VKEGDRVKAGDVLFQLDPTDYQAAldsaeaqlakaqaqvarlqael 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  170 ---QSEFLLLSGTGGTPTQIKGVLERLRlAGMPEEDIQrLRSTRTIQTRFTIKAPIDGVI--TAFDLRTGMNISKDKVVA 244
Cdd:pfam00529  82 drlQALESELAISRQDYDGATAQLRAAQ-AAVKAAQAQ-LAQAQIDLARRRVLAPIGGISreSLVTAGALVAQAQANLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  245 QIQGMDPVW--ISAAVPESIAYLLKDTSQFEISV--------PAYPDKTFHVEKW-------NILPSVDQTTRTLQVRLQ 307
Cdd:pfam00529 160 TVAQLDQIYvqITQSAAENQAEVRSELSGAQLQIaeaeaelkLAKLDLERTEIRApvdgtvaFLSVTVDGGTVSAGLRLM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  308 VSNKDE-FLKPGMNAYLKLNTQSQEM-LLIPSQAVIDT---GKEQRVITVDdeGKFVPKQIHVLHESQQQSGIGSGLNEG 382
Cdd:pfam00529 240 FVVPEDnLLVPGMFVETQLDQVRVGQpVLIPFDAFPQTktgRFTGVVVGIS--PDTGPVRVVVDKAQGPYYPLRIGLSAG 317


                  ....*
gi 486198972  383 DTVVV 387
Cdd:pfam00529 318 ALVRL 322
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
168-328 4.61e-12

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 66.61  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 168 EAQSEFLLLSGTGGTPTQIKGVLERLRLAgmpeedIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQ 247
Cdd:COG1566  166 AAQAQLAQAQAGLREEEELAAAQAQVAQA------EAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 248 GMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTF--HVEKwnILPSVDQTT----------RTLQVRLQVSNKD-EF 314
Cdd:COG1566  240 PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFegKVTS--ISPGAGFTSppknatgnvvQRYPVRIRLDNPDpEP 317

                        170
                 ....*....|....
gi 486198972 315 LKPGMNAYLKLNTQ 328
Cdd:COG1566  318 LRPGMSATVEIDTE 331
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 217-318 3.14e-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: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972  217 TIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVD 296
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80

                          90       100
                  ....*....|....*....|....
gi 486198972  297 QTTRTLQVRLQVSNKDE--FLKPG 318
Cdd:pfam13437  81 PDTGVIPVRVSIENPKTpiPLLPG 104
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
 50-77 2.77e-09

Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins.


Pssm-ID: 437167 [Multi-domain]  Cd Length: 28  Bit Score: 52.22  E-value: 2.77e-09
                          10        20
                  ....*....|....*....|....*...
gi 486198972   50 FWYDPMKPDTKFDKPGKSPFMDMDLVPK 77
Cdd:pfam19335   1 KYICPMHPDITSDKPGKCPICGMALVPV 28
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
218-390 2.56e-08

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 55.57  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 218 IKAPIDGVITAFDLRTGMNISKDK-----VVAQiqgMDPVWISAAVPES-IAYLLKDTSQfeisvpaypDKTFHVEKWN- 290
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQISSGDttgivVITQ---THPIDLVFTLPESdIATVVQAQKA---------GKPLVVEAWDr 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 291 ---------ILPSVDQ----TTRTLQVRLQVSNKDEFLKPG--MNAYLKLNTQsQEMLLIPSqAVIDTGKEQR-VITVDD 354
Cdd:PRK11556 266 tnskklsegTLLSLDNqidaTTGTIKLKARFNNQDDALFPNqfVNARMLVDTL-QNAVVIPT-AALQMGNEGHfVWVLND 343

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 486198972 355 EGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGL 390
Cdd:PRK11556 344 ENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGI 379
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
132-388 4.35e-06

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 48.64  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 132 VQARSDGFV-EKVYplTIGDHVKKGTPLIDITiPEWVEAQSEflllsgtggtptQIKGVLERLRLAGMPEEDIQR----L 206
Cdd:PRK09578  66 VRARVAGIVtARTY--EEGQEVKQGAVLFRID-PAPLKAARD------------AAAGALAKAEAAHLAALDKRRryddL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 207 RSTRTIQTR--------------------------------FTIKAPIDGVITAFDLRTGMNISKDKV--VAQIQGMDPV 252
Cdd:PRK09578 131 VRDRAVSERdyteavaderqakaavasakaelaraqlqldyATVTAPIDGRARRALVTEGALVGQDQAtpLTTVEQLDPI 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 253 WISAAVPESIAYLL---------KDTSQFEISVP-AYPDKTFHVEKWNILPS---VDQTTRTLQVRLQVSNKDEFLKPGm 319
Cdd:PRK09578 211 YVNFSQPAADVEALrravksgraTGIAQQDVAVTlVRADGSEYPLKGKLLFSdlaVDPTTDTVAMRALFPNPERELLPG- 289

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486198972 320 nAYLKLNTQS---QEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIhvlhESQQQSG----IGSGLNEGDTVVVS 388
Cdd:PRK09578 290 -AYVRIALDRavnPRAILVPRDALLRTADSASVKVVGQNGKVRDVEV----EADQMSGrdwiVTRGLAGGERVIVD 360
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
294-390 2.28e-05

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 46.25  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 294 SVDQTTRTLQVRLQVSNKDEFLKPGMNAYLKLNTQSQ-EMLLIPSQAVIDTGK-EQRVITVDDEGKFVPKQIHVLHESQQ 371
Cdd:PRK15030 266 TVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNpNAILVPQQGVTRTPRgDATVLVVGADDKVETRPIVASQAIGD 345

                         90
                 ....*....|....*....
gi 486198972 372 QSGIGSGLNEGDTVVVSGL 390
Cdd:PRK15030 346 KWLVTEGLKAGDRVVISGL 364
PRK09859 PRK09859
multidrug transporter subunit MdtE;
293-390 2.49e-05

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 46.25  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486198972 293 PSVDQTTRTLQVRLQVSNKDEFLKPGMNAYLKLNTQS-QEMLLIPSQAVIDTGKEQRVITVDDEGKFVP-KQIHVLHESQ 370
Cdd:PRK09859 261 PTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVTHNAQGKATALILDKDDVVQlREIEASKAIG 340

                         90       100
                 ....*....|....*....|
gi 486198972 371 QQSGIGSGLNEGDTVVVSGL 390
Cdd:PRK09859 341 DQWVVTSGLQAGDRVIVSGL 360
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH