|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
6-412 |
0e+00 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 830.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 6 IKYAAIIISSLIAGGLISVTAWQFVNSAQKAEKTEnTEKERKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADENEDK 85
Cdd:PRK09783 1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKT-STAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 86 SGSGIRIDPTQVQNLGLKTQKVSRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTTGDHVKKGTPLIDITIPE 165
Cdd:PRK09783 80 SSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 166 WVEAQSEFLLLSGTGGTPTQLKGVLERLRLAGMPEEDIQRLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQ 245
Cdd:PRK09783 160 WVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 246 IQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGMNAYLKL 325
Cdd:PRK09783 240 IQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 326 NTQSQEMLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALER 405
Cdd:PRK09783 320 NTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALER 399
|
....*..
gi 1758864856 406 MRHPEKT 412
Cdd:PRK09783 400 MRSESAT 406
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
111-321 |
6.58e-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: 245.88 E-value: 6.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 111 MLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTTGDHVKKGTPLIDITIPEWVEAQSEFLLLSGTGGTPTQ---LK 187
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 188 GVLERLRLAGMPEEDIQRLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLK 267
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1758864856 268 DTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGMNA 321
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
106-405 |
8.20e-55 |
|
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: 184.76 E-value: 8.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 106 KVSRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTTGDHVKKGTPLIDITIP----EWVEAQSEfllLSGTGG 181
Cdd:COG0845 2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPdlqaALAQAQAQ---LAAAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 182 TPTQLKGVLERLR-LAG---MPEEDIQ------------------RLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISK 239
Cdd:COG0845 76 QLELAKAELERYKaLLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 240 DKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGM 319
Cdd:COG0845 156 GTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 320 NAYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEAN 398
Cdd:COG0845 236 FVRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315
|
....*..
gi 1758864856 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 |
2.03e-31 |
|
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: 122.42 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 103 KTQKVSRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTTGDHVKKGTPLIDI-------------TIPEWVEA 169
Cdd:TIGR01730 2 TVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 170 QSEFL---------LLSGTGGTPTQLKGVLERLRLAgmpEEDIQRLRSTR---SIQTRFT-IKAPIDGVITAFDLRTGMN 236
Cdd:TIGR01730 79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAA---QADLEAAKASLasaQLNLRYTeIRAPFDGTIGRRLVEVGAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 237 ISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLK 316
Cdd:TIGR01730 156 VTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 317 PGMNAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVlheSQQQSG---IGSGLNEGDTVVVSGLFL 392
Cdd:TIGR01730 236 PGMFGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVK 312
|
.
gi 1758864856 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 |
6-412 |
0e+00 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 830.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 6 IKYAAIIISSLIAGGLISVTAWQFVNSAQKAEKTEnTEKERKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADENEDK 85
Cdd:PRK09783 1 MKKIALIIGSMIAGGIISAAGFTWVAKAEPPAEKT-STAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPKYADEESSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 86 SGSGIRIDPTQVQNLGLKTQKVSRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTTGDHVKKGTPLIDITIPE 165
Cdd:PRK09783 80 SSGGVRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 166 WVEAQSEFLLLSGTGGTPTQLKGVLERLRLAGMPEEDIQRLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQ 245
Cdd:PRK09783 160 WVEAQSEYLLLRETGGTATQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 246 IQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGMNAYLKL 325
Cdd:PRK09783 240 IQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 326 NTQSQEMLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALER 405
Cdd:PRK09783 320 NTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALER 399
|
....*..
gi 1758864856 406 MRHPEKT 412
Cdd:PRK09783 400 MRSESAT 406
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
111-321 |
6.58e-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: 245.88 E-value: 6.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 111 MLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTTGDHVKKGTPLIDITIPEWVEAQSEFLLLSGTGGTPTQ---LK 187
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKselLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 188 GVLERLRLAGMPEEDIQRLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLK 267
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1758864856 268 DTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGMNA 321
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
106-405 |
8.20e-55 |
|
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: 184.76 E-value: 8.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 106 KVSRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTTGDHVKKGTPLIDITIP----EWVEAQSEfllLSGTGG 181
Cdd:COG0845 2 KVERGDVPETVEATGTVEAR--REVEVRARVSGRVEEVL-VDEGDRVKKGQVLARLDPPdlqaALAQAQAQ---LAAAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 182 TPTQLKGVLERLR-LAG---MPEEDIQ------------------RLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISK 239
Cdd:COG0845 76 QLELAKAELERYKaLLKkgaVSQQELDqakaaldqaqaalaaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 240 DKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLKPGM 319
Cdd:COG0845 156 GTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 320 NAYLKLNT-QSQEMLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEAN 398
Cdd:COG0845 236 FVRVRIVLgERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315
|
....*..
gi 1758864856 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 |
2.03e-31 |
|
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: 122.42 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 103 KTQKVSRGMLNYSQTIPANVSYNeyQFVIVQARSDGFVEKVYpLTTGDHVKKGTPLIDI-------------TIPEWVEA 169
Cdd:TIGR01730 2 TVATVESETLANTLTFPGSLEAV--DEADLAAEVAGKITKIS-VREGQKVKKGQVLARLddddyqlalqaalAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 170 QSEFL---------LLSGTGGTPTQLKGVLERLRLAgmpEEDIQRLRSTR---SIQTRFT-IKAPIDGVITAFDLRTGMN 236
Cdd:TIGR01730 79 QLELAqrsferaerLVKRNAVSQADLDDAKAAVEAA---QADLEAAKASLasaQLNLRYTeIRAPFDGTIGRRLVEVGAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 237 ISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSADQTTRTLQVRLQVTNKDELLK 316
Cdd:TIGR01730 156 VTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 317 PGMNAYLKLNTQSQE-MLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIHVlheSQQQSG---IGSGLNEGDTVVVSGLFL 392
Cdd:TIGR01730 236 PGMFGRVTISLKVRSsAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEV---GLRNGGyveIESGLKAGDQIVTAGVVK 312
|
.
gi 1758864856 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 |
3.28e-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: 3.28e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1758864856 158 LIDITIPEWVEAQSEFLLLSGTGGTPTQLKGVLERLRLAGMPEEDIQRLRST 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 |
8.28e-13 |
|
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: 68.99 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 112 LNYSQTIPANVSYNEYQfVIVQARSDGFVEKVYpLTTGDHVKKGTPLIDITIPEWVEA---------------------- 169
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNA-KAVQPQVSGIVTRVL-VKEGDRVKAGDVLFQLDPTDYQAAldsaeaqlakaqaqvarlqael 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 170 ---QSEFLLLSGTGGTPTQLKGVLERLRlAGMPEEDIQrLRSTRSIQTRFTIKAPIDGVI--TAFDLRTGMNISKDKVVA 244
Cdd:pfam00529 82 drlQALESELAISRQDYDGATAQLRAAQ-AAVKAAQAQ-LAQAQIDLARRRVLAPIGGISreSLVTAGALVAQAQANLLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 245 QIQGMDPVW--ISAAVPESIAYLLKDTSQFEISV--------PAYPDKTFHVEKW-------NILPSADQTTRTLQVRLQ 307
Cdd:pfam00529 160 TVAQLDQIYvqITQSAAENQAEVRSELSGAQLQIaeaeaelkLAKLDLERTEIRApvdgtvaFLSVTVDGGTVSAGLRLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 308 VTNKDE-LLKPGMNAYLKLNTQSQEM-LLIPSQAVIDT---GKEQRVITVDDEGRfvPKKIHVLHESQQQSGIGSGLNEG 382
Cdd:pfam00529 240 FVVPEDnLLVPGMFVETQLDQVRVGQpVLIPFDAFPQTktgRFTGVVVGISPDTG--PVRVVVDKAQGPYYPLRIGLSAG 317
|
....*
gi 1758864856 383 DTVVV 387
Cdd:pfam00529 318 ALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
168-328 |
1.26e-12 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 68.54 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 168 EAQSEFLLLSGTGGTPTQLKGVLERLRLAgmpeedIQRLRSTRSIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQ 247
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQVAQA------EAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 248 GMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTF--HVEKwnILPSADQTT----------RTLQVRLQVTNKD-EL 314
Cdd:COG1566 240 PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFegKVTS--ISPGAGFTSppknatgnvvQRYPVRIRLDNPDpEP 317
|
170
....*....|....
gi 1758864856 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 |
3.27e-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: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 217 TIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSAD 296
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|....
gi 1758864856 297 QTTRTLQVRLQVTNKDE--LLKPG 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 1758864856 50 FWYDPMKPDTKFDKPGKSPFMDMDLVPK 77
Cdd:pfam19335 1 KYICPMHPDITSDKPGKCPICGMALVPV 28
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
218-390 |
4.32e-07 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 51.71 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 218 IKAPIDGVITAFDLRTGMNISKDK-----VVAQiqgMDPVWISAAVPES-IAYLLKDTSQfeisvpaypDKTFHVEKWN- 290
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQISSGDttgivVITQ---THPIDLVFTLPESdIATVVQAQKA---------GKPLVVEAWDr 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 291 ---------ILPSADQ----TTRTLQVRLQVTNKDELLKPG--MNAYLKLNTQsQEMLLIPSqAVIDTGKEQRVITVDDE 355
Cdd:PRK11556 266 tnskklsegTLLSLDNqidaTTGTIKLKARFNNQDDALFPNqfVNARMLVDTL-QNAVVIPT-AALQMGNEGHFVWVLND 343
|
170 180 190
....*....|....*....|....*....|....*..
gi 1758864856 356 GRFVPKKIhVLHESQ--QQSGIGSGLNEGDTVVVSGL 390
Cdd:PRK11556 344 ENKVSKHL-VTPGIQdsQKVVISAGLSAGDRVVTDGI 379
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
132-388 |
5.00e-05 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 45.17 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 132 VQARSDGFV-EKVYplTTGDHVKKGTPLIDITiPEWVEAQSEflllsgtggtptQLKGVLERLRLAGMPEEDIQR----L 206
Cdd:PRK09578 66 VRARVAGIVtARTY--EEGQEVKQGAVLFRID-PAPLKAARD------------AAAGALAKAEAAHLAALDKRRryddL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 207 RSTRSIQTR--------------------------------FTIKAPIDGVITAFDLRTGMNISKDKV--VAQIQGMDPV 252
Cdd:PRK09578 131 VRDRAVSERdyteavaderqakaavasakaelaraqlqldyATVTAPIDGRARRALVTEGALVGQDQAtpLTTVEQLDPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 253 WISAAVPESIAYLL---------KDTSQFEISVP-AYPDKTFHVEKWNILPS---ADQTTRTLQVRLQVTNKDELLKPGm 319
Cdd:PRK09578 211 YVNFSQPAADVEALrravksgraTGIAQQDVAVTlVRADGSEYPLKGKLLFSdlaVDPTTDTVAMRALFPNPERELLPG- 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758864856 320 nAYLKLNTQS---QEMLLIPSQAVIDTGKEQRVITVDDEGRFVPKKIhvlhESQQQSG----IGSGLNEGDTVVVS 388
Cdd:PRK09578 290 -AYVRIALDRavnPRAILVPRDALLRTADSASVKVVGQNGKVRDVEV----EADQMSGrdwiVTRGLAGGERVIVD 360
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
293-390 |
1.99e-04 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 43.55 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 293 PSADQTTRTLQVRLQVTNKDELLKPGMNAYLKLNTQS-QEMLLIPSQAVIDTGKEQRVITVDDEGRFVP-KKIHVLHESQ 370
Cdd:PRK09859 261 PTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVTHNAQGKATALILDKDDVVQlREIEASKAIG 340
|
90 100
....*....|....*....|
gi 1758864856 371 QQSGIGSGLNEGDTVVVSGL 390
Cdd:PRK09859 341 DQWVVTSGLQAGDRVIVSGL 360
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
294-390 |
6.02e-04 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 42.01 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758864856 294 SADQTTRTLQVRLQVTNKDELLKPGMNAYLKLNTQSQ-EMLLIPSQAVIDTGK-EQRVITVDDEGRFVPKKIHVLHESQQ 371
Cdd:PRK15030 266 TVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNpNAILVPQQGVTRTPRgDATVLVVGADDKVETRPIVASQAIGD 345
|
90
....*....|....*....
gi 1758864856 372 QSGIGSGLNEGDTVVVSGL 390
Cdd:PRK15030 346 KWLVTEGLKAGDRVVISGL 364
|
|
| |
