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Conserved domains on  [gi|1867952959|ref|WP_179020713|]
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efflux RND transporter periplasmic adaptor subunit [Winogradskyella forsetii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 113-322 5.71e-90

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: 277.08  E-value: 5.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 113 NNSLKLSGKIKANEESNAVQVTYFGGRIEKLYVNSTGERVGAGQRLATIYSPELVAAQQELLTASSLKESQP--ELYKAV 190
Cdd:pfam16576   3 SRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSksELLRAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 191 RNKLKLWKLSEKQINAIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEG 270
Cdd:pfam16576  83 RQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1867952959 271 QTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFV 322
Cdd:pfam16576 163 QPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
 463-556 7.12e-33

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


:

Pssm-ID: 432106  Cd Length: 93  Bit Score: 121.34  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 463 VFDDYILLKDALVNDDAKGAQQAGKQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANTIENNSDIATQRAHFKHLSA 542
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79

                          90
                  ....*....|....
gi 1867952959 543 HMISSVQLFGVNEN 556
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
 51-77 3.77e-11

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: 57.61  E-value: 3.77e-11
                          10        20
                  ....*....|....*....|....*..
gi 1867952959  51 WTCSMHPQIMQPEPGDCPICGMDLIPA 77
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
 
Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 113-322 5.71e-90

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: 277.08  E-value: 5.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 113 NNSLKLSGKIKANEESNAVQVTYFGGRIEKLYVNSTGERVGAGQRLATIYSPELVAAQQELLTASSLKESQP--ELYKAV 190
Cdd:pfam16576   3 SRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSksELLRAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 191 RNKLKLWKLSEKQINAIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEG 270
Cdd:pfam16576  83 RQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1867952959 271 QTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFV 322
Cdd:pfam16576 163 QPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 115-411 4.19e-73

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: 237.15  E-value: 4.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 115 SLKLSGKIKANEESN-AVQVtyfGGRIEKLYVNsTGERVGAGQRLATIYSP----ELVAAQQELLTA-SSLKESQPELyk 188
Cdd:COG0845    11 TVEATGTVEARREVEvRARV---SGRVEEVLVD-EGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAqAQLELAKAEL-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 189 aVRNKlKLWK---LSEKQIN------------------AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKI 247
Cdd:COG0845    85 -ERYK-ALLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 248 ANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEGIIE 327
Cdd:COG0845   163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 328 GTQtrTENTVSVPSTAVMWTGERSVVYVKTNPNeaIFEMREVLLGNANGDSYTILEGLKNGDEVVTNGTFTVDAAAQLQG 407
Cdd:COG0845   243 LGE--RENALLVPASAVVRDGGGAYVFVVDADG--KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRV 318


                  ....
gi 1867952959 408 KKSM 411
Cdd:COG0845   319 VEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 106-399 2.59e-43

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: 157.48  E-value: 2.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 106 VGKGQMgNNSLKLSGKIKANEESN-AVQVtyfGGRIEKLYVNStGERVGAGQRLATIYSPELVAAQQELLTASSLKESQP 184
Cdd:TIGR01730   6 VESETL-ANTLTFPGSLEAVDEADlAAEV---AGKITKISVRE-GQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 185 ELYKAVRNKL-KLWK---LSEKQIN------------------AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQ 242
Cdd:TIGR01730  81 ELAQRSFERAeRLVKrnaVSQADLDdakaaveaaqadleaakaSLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 243 PLYKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFV 322
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867952959 323 EGIIEGTQtrTENTVSVPSTAVMWTGERSVVYVKTNPNEAifEMREVLLGNANGDSYTILEGLKNGDEVVTNGTFTV 399
Cdd:TIGR01730 241 RVTISLKV--RSSAIVVPTQAVIEDLNGKYVYVVKNDGKV--SKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
 463-556 7.12e-33

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


Pssm-ID: 432106  Cd Length: 93  Bit Score: 121.34  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 463 VFDDYILLKDALVNDDAKGAQQAGKQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANTIENNSDIATQRAHFKHLSA 542
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79

                          90
                  ....*....|....
gi 1867952959 543 HMISSVQLFGVNEN 556
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 51-416 2.49e-28

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 117.66  E-value: 2.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959  51 WTCSMHPQIMQPEPGDCPICGMDLIP--AESGADGLNANeIKMTDNAMALANIQTSLVGKGQMgNNSLKLSGKIKANEES 128
Cdd:PRK09783   45 WYDPMYPNTRFDKPGKSPFMDMDLVPkyADEESSASSGG-VRIDPTQTQNLGVKTATVTRGPL-TFAQTFPANVSYNEYQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 129 NAVQVTYFGGRIEKLYVNSTGERVGAGQRLATIYSPELVAAQQELLTASSlKESQPELYKAVRNKLKLWKLSEKQINAIE 208
Cdd:PRK09783  123 YAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDWVEAQSEYLLLRE-TGGTATQTEGILERLRLAGMPEADIRRLI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 209 TAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAK 288
Cdd:PRK09783  202 ATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 289 VSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEGIIEgtqTRTENTVSVPSTAVMWTG-ERSVVYVKtnpNEAIFEMR 367
Cdd:PRK09783  282 KWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLN---TASEPMLLIPSQALIDTGsEQRVITVD---ADGRFVPK 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1867952959 368 EVLLGNANGDSYTILEGLKNGDEVVTNGTFTVDAAAQLQGKKSMMNASG 416
Cdd:PRK09783  356 RVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERMRSES 404
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
 51-77 3.77e-11

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: 57.61  E-value: 3.77e-11
                          10        20
                  ....*....|....*....|....*..
gi 1867952959  51 WTCSMHPQIMQPEPGDCPICGMDLIPA 77
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
 
Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 113-322 5.71e-90

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: 277.08  E-value: 5.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 113 NNSLKLSGKIKANEESNAVQVTYFGGRIEKLYVNSTGERVGAGQRLATIYSPELVAAQQELLTASSLKESQP--ELYKAV 190
Cdd:pfam16576   3 SRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSksELLRAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 191 RNKLKLWKLSEKQINAIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEG 270
Cdd:pfam16576  83 RQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1867952959 271 QTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFV 322
Cdd:pfam16576 163 QPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 115-411 4.19e-73

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: 237.15  E-value: 4.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 115 SLKLSGKIKANEESN-AVQVtyfGGRIEKLYVNsTGERVGAGQRLATIYSP----ELVAAQQELLTA-SSLKESQPELyk 188
Cdd:COG0845    11 TVEATGTVEARREVEvRARV---SGRVEEVLVD-EGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAqAQLELAKAEL-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 189 aVRNKlKLWK---LSEKQIN------------------AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKI 247
Cdd:COG0845    85 -ERYK-ALLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 248 ANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEGIIE 327
Cdd:COG0845   163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 328 GTQtrTENTVSVPSTAVMWTGERSVVYVKTNPNeaIFEMREVLLGNANGDSYTILEGLKNGDEVVTNGTFTVDAAAQLQG 407
Cdd:COG0845   243 LGE--RENALLVPASAVVRDGGGAYVFVVDADG--KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRV 318


                  ....
gi 1867952959 408 KKSM 411
Cdd:COG0845   319 VEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 106-399 2.59e-43

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: 157.48  E-value: 2.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 106 VGKGQMgNNSLKLSGKIKANEESN-AVQVtyfGGRIEKLYVNStGERVGAGQRLATIYSPELVAAQQELLTASSLKESQP 184
Cdd:TIGR01730   6 VESETL-ANTLTFPGSLEAVDEADlAAEV---AGKITKISVRE-GQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 185 ELYKAVRNKL-KLWK---LSEKQIN------------------AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQ 242
Cdd:TIGR01730  81 ELAQRSFERAeRLVKrnaVSQADLDdakaaveaaqadleaakaSLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 243 PLYKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFV 322
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867952959 323 EGIIEGTQtrTENTVSVPSTAVMWTGERSVVYVKTNPNEAifEMREVLLGNANGDSYTILEGLKNGDEVVTNGTFTV 399
Cdd:TIGR01730 241 RVTISLKV--RSSAIVVPTQAVIEDLNGKYVYVVKNDGKV--SKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
 463-556 7.12e-33

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


Pssm-ID: 432106  Cd Length: 93  Bit Score: 121.34  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 463 VFDDYILLKDALVNDDAKGAQQAGKQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANTIENNSDIATQRAHFKHLSA 542
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79

                          90
                  ....*....|....
gi 1867952959 543 HMISSVQLFGVNEN 556
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 51-416 2.49e-28

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 117.66  E-value: 2.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959  51 WTCSMHPQIMQPEPGDCPICGMDLIP--AESGADGLNANeIKMTDNAMALANIQTSLVGKGQMgNNSLKLSGKIKANEES 128
Cdd:PRK09783   45 WYDPMYPNTRFDKPGKSPFMDMDLVPkyADEESSASSGG-VRIDPTQTQNLGVKTATVTRGPL-TFAQTFPANVSYNEYQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 129 NAVQVTYFGGRIEKLYVNSTGERVGAGQRLATIYSPELVAAQQELLTASSlKESQPELYKAVRNKLKLWKLSEKQINAIE 208
Cdd:PRK09783  123 YAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDWVEAQSEYLLLRE-TGGTATQTEGILERLRLAGMPEADIRRLI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 209 TAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAK 288
Cdd:PRK09783  202 ATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 289 VSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEGIIEgtqTRTENTVSVPSTAVMWTG-ERSVVYVKtnpNEAIFEMR 367
Cdd:PRK09783  282 KWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLN---TASEPMLLIPSQALIDTGsEQRVITVD---ADGRFVPK 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1867952959 368 EVLLGNANGDSYTILEGLKNGDEVVTNGTFTVDAAAQLQGKKSMMNASG 416
Cdd:PRK09783  356 RVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERMRSES 404
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
165-327 1.71e-20

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 92.80  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 165 ELVAAQQELLTASSLKESQPELyKAVRNKLKLWKLSEKQINaietagkvqenfpVFATVSGTVTMKMVEEGDYLKQGQPL 244
Cdd:COG1566   170 QLAQAQAGLREEEELAAAQAQV-AQAEAALAQAELNLARTT-------------IRAPVDGVVTNLNVEPGEVVSAGQPL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 245 YKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNSAT----------RTVVVRAVLQNK-K 313
Cdd:COG1566   236 LTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSppknatgnvvQRYPVRIRLDNPdP 315

                         170
                  ....*....|....
gi 1867952959 314 DLFKPGMFVEGIIE 327
Cdd:COG1566   316 EPLRPGMSATVEID 329
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 219-319 4.71e-17

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: 77.02  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 219 VFATVSGTVTMKMVEEGDYLKQGQPLYKIANLNTVWAEFDAYENQIASLKEGQTIKVTTNAYRNEVFDAKVSFIDPLLNS 298
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVDP 81

                          90       100
                  ....*....|....*....|...
gi 1867952959 299 ATRTVVVRAVL--QNKKDLFKPG 319
Cdd:pfam13437  82 DTGVIPVRVSIenPKTPIPLLPG 104
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 118-393 1.49e-11

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: 65.91  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 118 LSGKIKANEESNAV--QVtyfGGRIEKLYVNStGERVGAGQRLATIYSPELVAAQQELLTASSLKESQPELYKAVRNKLK 195
Cdd:pfam00529  10 APGRVVVSGNAKAVqpQV---SGIVTRVLVKE-GDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 196 LWKL----SEKQIN------------------AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQP--LYKIANLN 251
Cdd:pfam00529  86 ALESelaiSRQDYDgataqlraaqaavkaaqaQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnlLATVAQLD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 252 TVWAEFDAYENQIASLKEGQTIKVTT--NAYRNEV---------------FDAKVSFIDPLLNSATRTVVVRAVLQNK-K 313
Cdd:pfam00529 166 QIYVQITQSAAENQAEVRSELSGAQLqiAEAEAELklakldlerteirapVDGTVAFLSVTVDGGTVSAGLRLMFVVPeD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 314 DLFKPGMFVEGIIEgtQTRTENTVSVPSTAVMwTGERSVVYVKTNPNEAIFEMREVLLGNANGDSYTILEGLKNGDEVVT 393
Cdd:pfam00529 246 NLLVPGMFVETQLD--QVRVGQPVLIPFDAFP-QTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
 51-77 3.77e-11

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: 57.61  E-value: 3.77e-11
                          10        20
                  ....*....|....*....|....*..
gi 1867952959  51 WTCSMHPQIMQPEPGDCPICGMDLIPA 77
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
206-409 8.45e-11

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 63.96  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 206 AIETAGKVQENFPVFATVSGTVTMKMVEEGDYLKQGQP--LYKIANLNTVWAEFDAYENQIASLKEgqtiKVTTNAYRNE 283
Cdd:PRK15030  163 AVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPIYVDVTQSSNDFLRLKQ----ELANGTLKQE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 284 VFDAKVS----------------FIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEGII-EGTQTrteNTVSVPSTAVMW 346
Cdd:PRK15030  239 NGKAKVSlitsdgikfpqdgtleFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLeEGLNP---NAILVPQQGVTR 315

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867952959 347 T--GERSVVYVKTNPNeaiFEMREVLLGNANGDSYTILEGLKNGDEVVTNGTFTVDAAAQLQGKK 409
Cdd:PRK15030  316 TprGDATVLVVGADDK---VETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQE 377
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
149-395 1.82e-08

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 56.72  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 149 GERVGAGQRLATI----YSPELVAAQQEL-------------------LTASSLKeSQPELykavRNKLKLWKLSEKQIN 205
Cdd:PRK11556  106 GQQVKAGDLLAEIdprpFKVALAQAQGQLakdqatlanarrdlaryqqLAKTNLV-SRQEL----DAQQALVSETEGTIK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 206 AIETA---GKVQENFP-VFATVSGTVTMKMVEEGDYLKQGQ--PLYKIANLNTVWAEFDAYENQIASL----KEGQTIKV 275
Cdd:PRK11556  181 ADEASvasAQLQLDYSrITAPISGRVGLKQVDVGNQISSGDttGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLVV 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 276 T----TNayRNEVFDAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEG-IIEGTQtrtENTVSVPSTAVMWTGER 350
Cdd:PRK11556  261 EawdrTN--SKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNArMLVDTL---QNAVVIPTAALQMGNEG 335

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1867952959 351 SVVYVKTNPNEAifEMREVLLGNANGDSYTILEGLKNGDEVVTNG 395
Cdd:PRK11556  336 HFVWVLNDENKV--SKHLVTPGIQDSQKVVISAGLSAGDRVVTDG 378
PRK09859 PRK09859
multidrug transporter subunit MdtE;
222-395 2.95e-07

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 52.79  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 222 TVSGTVTMKMVEEGDYLKQGQPLYkiANLNTVWAEFDAYENQIASLK----EGQT-IKVTTNAYRNEVFDAKVSFIDPLL 296
Cdd:PRK09859  186 TVGALVTANQADSLVTVQRLDPIY--VDLTQSVQDFLRMKEEVASGQikqvQGSTpVQLNLENGKRYSQTGTLKFSDPTV 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 297 NSATRTVVVRAVLQNKKDLFKPGMFVEGII-EGTQtrtENTVSVPSTAVMWTGERSVVYVKTNPNEAIfEMREVLLGNAN 375
Cdd:PRK09859  264 DETTGSVTLRAIFPNPNGDLLPGMYVTALVdEGSR---QNVLLVPQEGVTHNAQGKATALILDKDDVV-QLREIEASKAI 339

                         170       180
                  ....*....|....*....|
gi 1867952959 376 GDSYTILEGLKNGDEVVTNG 395
Cdd:PRK09859  340 GDQWVVTSGLQAGDRVIVSG 359
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
219-405 1.11e-06

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 50.95  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 219 VFATVSGTVTMKMVEEGDYLKQGQ--PLYKIANLNTVWAEFDAYENQIASL----KEGQT-------IKVTT-----NAY 280
Cdd:PRK09578  174 VTAPIDGRARRALVTEGALVGQDQatPLTTVEQLDPIYVNFSQPAADVEALrravKSGRAtgiaqqdVAVTLvradgSEY 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 281 RNEvfdAKVSFIDPLLNSATRTVVVRAVLQNKKDLFKPGMFVEgiIEGTQTRTENTVSVPSTAVMWTGERSVVYVkTNPN 360
Cdd:PRK09578  254 PLK---GKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVR--IALDRAVNPRAILVPRDALLRTADSASVKV-VGQN 327

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867952959 361 EAIFEMrEVLLGNANGDSYTILEGLKNGDEVVtngtftVDAAAQL 405
Cdd:PRK09578  328 GKVRDV-EVEADQMSGRDWIVTRGLAGGERVI------VDNAAQF 365
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
196-291 1.66e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 47.35  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867952959 196 LWKLSEKQINAIETA-GKVQENF-PVFATVSGTVTMKMVEEGDYLKQGQPLYKI------ANLNTVWAEFDAYENQIASL 267
Cdd:COG1566    23 LWAAGRNGPDEPVTAdGRVEARVvTVAAKVSGRVTEVLVKEGDRVKKGQVLARLdptdlqAALAQAEAQLAAAEAQLARL 102

                          90       100
                  ....*....|....*....|....
gi 1867952959 268 KEGQTIKVTTNAYRNEVFDAKVSF 291
Cdd:COG1566   103 EAELGAEAEIAAAEAQLAAAQAQL 126
 
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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