|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
6-409 |
0e+00 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 797.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 6 IKYAAVIASSLIAGGLISVTAWQALHSSEKTENSA--SERKVLFWYDPMKPDVKFDKPGKSPFMDMDLVPKYADENANKN 83
Cdd:PRK09783 1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTstAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 84 SAGIRIDPTQVQNLGLKTQKVTRGTLSYAQTIPANVSYNDYQFVIVQARAEGFVEKVYPLTTGDKVKKGTPLVDITIPDW 163
Cdd:PRK09783 81 SGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 164 VEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKVVAQI 243
Cdd:PRK09783 161 VEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 244 QGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGMNAYLKLN 323
Cdd:PRK09783 241 QGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 324 TQSQEMLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVLHESQQQSGIGSGLEEGESVVVSGLFLIDSEANITGALERM 403
Cdd:PRK09783 321 TASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERM 400
|
....*.
gi 2105025853 404 RHTEAA 409
Cdd:PRK09783 401 RSESAT 406
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
108-318 |
5.82e-76 |
|
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: 235.09 E-value: 5.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 108 TLSYAQTIPANVSYNDYQFVIVQARAEGFVEKVYPLTTGDKVKKGTPLVDITIPDWVEAQSEFLLLSGTGGTPTQ---IK 184
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 185 GVLERLRLAGMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKVVAQIQGMDPVWIGAAVPESIAYLLK 264
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105025853 265 ETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGMNA 318
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
103-402 |
5.13e-50 |
|
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: 171.66 E-value: 5.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 103 KVTRGTLSYAQTIPANVSYNdyQFVIVQARAEGFVEKVYpLTTGDKVKKGTPLVDITIPD----WVEAQSEFL------- 171
Cdd:COG0845 2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPDlqaaLAQAQAQLAaaqaqle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 172 -----------LLSGTGGTPTQIKGVLERLRLA-GMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKV 239
Cdd:COG0845 79 lakaelerykaLLKKGAVSQQELDQAKAALDQAqAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 240 VAQIQGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFP--VDKWSllPSVDPTTRTLQVRLQISNRDELLKPGMN 317
Cdd:COG0845 159 LFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEgkVTFID--PAVDPATRTVRVRAELPNPDGLLRPGMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 318 AYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVLHESQQQSGIGSGLEEGESVVVSGLFLIDSEANI 396
Cdd:COG0845 237 VRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKV 316
|
....*.
gi 2105025853 397 TGALER 402
Cdd:COG0845 317 RVVEAA 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
100-390 |
6.94e-25 |
|
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: 103.93 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 100 KTQKVTRGTLSYAQTIPANVSYNDYqfVIVQARAEGFVEKVYpLTTGDKVKKGTPLVDI-------------TIPDWVEA 166
Cdd:TIGR01730 2 TVATVESETLANTLTFPGSLEAVDE--ADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 167 QSEFL---------LLSGTGGTPTQIKGVLERLRLA-GMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISK 236
Cdd:TIGR01730 79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAAqADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 237 DKVVAQIQGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGM 316
Cdd:TIGR01730 159 GQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGM 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105025853 317 NAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVlheSQQQSG---IGSGLEEGESVVVSGLFLI 390
Cdd:TIGR01730 239 FGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVKL 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
6-409 |
0e+00 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 797.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 6 IKYAAVIASSLIAGGLISVTAWQALHSSEKTENSA--SERKVLFWYDPMKPDVKFDKPGKSPFMDMDLVPKYADENANKN 83
Cdd:PRK09783 1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKTstAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 84 SAGIRIDPTQVQNLGLKTQKVTRGTLSYAQTIPANVSYNDYQFVIVQARAEGFVEKVYPLTTGDKVKKGTPLVDITIPDW 163
Cdd:PRK09783 81 SGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 164 VEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKVVAQI 243
Cdd:PRK09783 161 VEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 244 QGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGMNAYLKLN 323
Cdd:PRK09783 241 QGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 324 TQSQEMLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVLHESQQQSGIGSGLEEGESVVVSGLFLIDSEANITGALERM 403
Cdd:PRK09783 321 TASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERM 400
|
....*.
gi 2105025853 404 RHTEAA 409
Cdd:PRK09783 401 RSESAT 406
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
108-318 |
5.82e-76 |
|
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: 235.09 E-value: 5.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 108 TLSYAQTIPANVSYNDYQFVIVQARAEGFVEKVYPLTTGDKVKKGTPLVDITIPDWVEAQSEFLLLSGTGGTPTQ---IK 184
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 185 GVLERLRLAGMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKVVAQIQGMDPVWIGAAVPESIAYLLK 264
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105025853 265 ETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGMNA 318
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
103-402 |
5.13e-50 |
|
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: 171.66 E-value: 5.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 103 KVTRGTLSYAQTIPANVSYNdyQFVIVQARAEGFVEKVYpLTTGDKVKKGTPLVDITIPD----WVEAQSEFL------- 171
Cdd:COG0845 2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPDlqaaLAQAQAQLAaaqaqle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 172 -----------LLSGTGGTPTQIKGVLERLRLA-GMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKV 239
Cdd:COG0845 79 lakaelerykaLLKKGAVSQQELDQAKAALDQAqAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 240 VAQIQGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFP--VDKWSllPSVDPTTRTLQVRLQISNRDELLKPGMN 317
Cdd:COG0845 159 LFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEgkVTFID--PAVDPATRTVRVRAELPNPDGLLRPGMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 318 AYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVLHESQQQSGIGSGLEEGESVVVSGLFLIDSEANI 396
Cdd:COG0845 237 VRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKV 316
|
....*.
gi 2105025853 397 TGALER 402
Cdd:COG0845 317 RVVEAA 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
100-390 |
6.94e-25 |
|
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: 103.93 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 100 KTQKVTRGTLSYAQTIPANVSYNDYqfVIVQARAEGFVEKVYpLTTGDKVKKGTPLVDI-------------TIPDWVEA 166
Cdd:TIGR01730 2 TVATVESETLANTLTFPGSLEAVDE--ADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 167 QSEFL---------LLSGTGGTPTQIKGVLERLRLA-GMPDEDIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISK 236
Cdd:TIGR01730 79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAAqADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 237 DKVVAQIQGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFPVDKWSLLPSVDPTTRTLQVRLQISNRDELLKPGM 316
Cdd:TIGR01730 159 GQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGM 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105025853 317 NAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDADGNFVPKRIHVlheSQQQSG---IGSGLEEGESVVVSGLFLI 390
Cdd:TIGR01730 239 FGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVKL 313
|
|
| HlyD_D4 |
pfam16572 |
Long alpha hairpin domain of cation efflux system protein, CusB; HlyD_D4 is the long ... |
155-206 |
1.27e-18 |
|
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: 79.23 E-value: 1.27e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2105025853 155 LVDITIPDWVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPDEDIQRLRAT 206
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 ... |
106-384 |
3.04e-15 |
|
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: 75.92 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 106 RGTLSYAQTIPANVSYNDYQfVIVQARAEGFVEKVYpLTTGDKVKKGTPLVDITIPDWVEA------------------- 166
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNA-KAVQPQVSGIVTRVL-VKEGDRVKAGDVLFQLDPTDYQAAldsaeaqlakaqaqvarlq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 167 ------QSEFLLLSGTGGTPTQIKGVLERLRlAGMPDEDIQrLRATRTIQTRFTIRAPIDGAI--TAFDLRTGMNISKDK 238
Cdd:pfam00529 79 aeldrlQALESELAISRQDYDGATAQLRAAQ-AAVKAAQAQ-LAQAQIDLARRRVLAPIGGISreSLVTAGALVAQAQAN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 239 VVAQIQGMDPVW--IGAAVPESIAYLLKETSQFAVSI--------PAYPDKSF-----PVDKW--SLLPSVDPTTRTLQV 301
Cdd:pfam00529 157 LLATVAQLDQIYvqITQSAAENQAEVRSELSGAQLQIaeaeaelkLAKLDLERteiraPVDGTvaFLSVTVDGGTVSAGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 302 RL-QISNRDELLKPGMNAYLKLNTQSQEM-LLIPSQAVIDT---GKEQRVITVDADGnfVPKRIHVLHESQQQSGIGSGL 376
Cdd:pfam00529 237 RLmFVVPEDNLLVPGMFVETQLDQVRVGQpVLIPFDAFPQTktgRFTGVVVGISPDT--GPVRVVVDKAQGPYYPLRIGL 314
|
....*...
gi 2105025853 377 EEGESVVV 384
Cdd:pfam00529 315 SAGALVRL 322
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
214-315 |
1.02e-09 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 55.45 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 214 TIRAPIDGAITAFDLRTGMNISKDKVVAQIQGMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFPVDKWSLLPSVD 293
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|....
gi 2105025853 294 PTTRTLQVRLQISNRDE--LLKPG 315
Cdd:pfam13437 81 PDTGVIPVRVSIENPKTpiPLLPG 104
|
|
| HMBD |
pfam19335 |
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ... |
47-74 |
1.06e-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: 53.37 E-value: 1.06e-09
10 20
....*....|....*....|....*...
gi 2105025853 47 FWYDPMKPDVKFDKPGKSPFMDMDLVPK 74
Cdd:pfam19335 1 KYICPMHPDITSDKPGKCPICGMALVPV 28
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
165-325 |
2.19e-09 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 58.52 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 165 EAQSEFLLLSGTGGTPTQIKGVLERLRLAgmpdedIQRLRATRTIQTRFTIRAPIDGAITAFDLRTGMNISKDKVVAQIQ 244
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQVAQA------EAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 245 GMDPVWIGAAVPESIAYLLKETSQFAVSIPAYPDKSFP--VDkwSLLPSVDPTT----------RTLQVRLQISNRD-EL 311
Cdd:COG1566 240 PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEgkVT--SISPGAGFTSppknatgnvvQRYPVRIRLDNPDpEP 317
|
170
....*....|....
gi 2105025853 312 LKPGMNAYLKLNTQ 325
Cdd:COG1566 318 LRPGMSATVEIDTE 331
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
215-387 |
3.21e-08 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 55.18 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 215 IRAPIDGAITAFDLRTGMNISKDK-----VVAQiqgMDPVWIGAAVPES-IAYLLKetSQFAvsipaypDKSFPVDKW-- 286
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQISSGDttgivVITQ---THPIDLVFTLPESdIATVVQ--AQKA-------GKPLVVEAWdr 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 287 ------------SLLPSVDPTTRTLQVRLQISNRDELLKPG--MNAYLKLNTQsQEMLLIPSqAVIDTGKEQRVITVDAD 352
Cdd:PRK11556 266 tnskklsegtllSLDNQIDATTGTIKLKARFNNQDDALFPNqfVNARMLVDTL-QNAVVIPT-AALQMGNEGHFVWVLND 343
|
170 180 190
....*....|....*....|....*....|....*..
gi 2105025853 353 GNFVPKRIhVLHESQ--QQSGIGSGLEEGESVVVSGL 387
Cdd:PRK11556 344 ENKVSKHL-VTPGIQdsQKVVISAGLSAGDRVVTDGI 379
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
215-387 |
5.83e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 45.09 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 215 IRAPIDGAITAFDLRTGMNISKDKV--VAQIQGMDPVWIGAA--------VPESIA--YLLKETSQFAVSIPAYPDKSFP 282
Cdd:PRK15030 176 VTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPIYVDVTqssndflrLKQELAngTLKQENGKAKVSLITSDGIKFP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 283 VD---KWSLLpSVDPTTRTLQVRLQISNRDELLKPGMNAYLKLNTQSQ-EMLLIPSQAVIDTGK-EQRVITVDADGNFVP 357
Cdd:PRK15030 256 QDgtlEFSDV-TVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNpNAILVPQQGVTRTPRgDATVLVVGADDKVET 334
|
170 180 190
....*....|....*....|....*....|
gi 2105025853 358 KRIHVLHESQQQSGIGSGLEEGESVVVSGL 387
Cdd:PRK15030 335 RPIVASQAIGDKWLVTEGLKAGDRVVISGL 364
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
291-385 |
6.93e-05 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 44.78 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 291 SVDPTTRTLQVRLQISNRDELLKPGMNAYLKLNTQ-SQEMLLIPSQAVIDTGKEQRVITVDADGNFVPkrihVLHESQQQ 369
Cdd:PRK09578 265 AVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAvNPRAILVPRDALLRTADSASVKVVGQNGKVRD----VEVEADQM 340
|
90 100
....*....|....*....|
gi 2105025853 370 SG----IGSGLEEGESVVVS 385
Cdd:PRK09578 341 SGrdwiVTRGLAGGERVIVD 360
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
290-387 |
1.92e-04 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 43.16 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105025853 290 PSVDPTTRTLQVRLQISNRDELLKPGMNAYLKLNTQS-QEMLLIPSQAVIDT--GKEQRVItVDADGNFVPKRIHVLHES 366
Cdd:PRK09859 261 PTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVTHNaqGKATALI-LDKDDVVQLREIEASKAI 339
|
90 100
....*....|....*....|.
gi 2105025853 367 QQQSGIGSGLEEGESVVVSGL 387
Cdd:PRK09859 340 GDQWVVTSGLQAGDRVIVSGL 360
|
|
| |
