|
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 ... |
116-325 |
5.36e-95 |
|
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: 289.41 E-value: 5.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 116 ALSPRIETVGYVAFDESALWQTNVRVSGWVEKLSINAVGEKVNKGDVLFTLYSPELVKAQDELISAYKTGRKG----LIK 191
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALskseLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 192 GSTERLITLGVDKTQIRSITRKGKASQTIEVKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWIS 271
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497531327 272 SGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| CusF_Ec |
pfam11604 |
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ... |
505-571 |
1.06e-19 |
|
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.
:
Pssm-ID: 463306 Cd Length: 68 Bit Score: 83.02 E-value: 1.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 505 GDITMLMADFGMITVKHQPVPEWNWKAGEMNFQASDDLDLSEFAEGQTIRFLVAKQGS-DYVLKSLEP 571
Cdd:pfam11604 1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPALLAGLKPGDKVRFEFEKDDGgEYTITKIEP 68
|
|
| CusF |
COG5569 |
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]; |
413-491 |
6.53e-19 |
|
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
:
Pssm-ID: 444311 Cd Length: 101 Bit Score: 81.96 E-value: 6.53e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497531327 413 SVEEEAETVWANGEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDFEMRKTESGRYEVVDYK 491
Cdd:COG5569 20 AAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPALLKGLKVGDKVRFEFERVGDGGYVITSIE 98
|
|
| HMBD |
pfam19335 |
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ... |
53-79 |
5.71e-07 |
|
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: 46.05 E-value: 5.71e-07
10 20
....*....|....*....|....*...
gi 497531327 53 YWVAPMDPNYQRDKPGQSP-MGMDLIPV 79
Cdd:pfam19335 1 KYICPMHPDITSDKPGKCPiCGMALVPV 28
|
|
| PRK09578 super family |
cl31598 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
300-420 |
9.55e-07 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
The actual alignment was detected with superfamily member PRK09578:
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 51.33 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 300 DPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIE 379
Cdd:PRK09578 267 DPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWI 346
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 497531327 380 VLQGLEQGENIVTsahfmldSESSQSADLSRINSVEEEAET 420
Cdd:PRK09578 347 VTRGLAGGERVIV-------DNAAQFAPGTAVKAVERAPAA 380
|
|
| |
|
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 ... |
116-325 |
5.36e-95 |
|
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: 289.41 E-value: 5.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 116 ALSPRIETVGYVAFDESALWQTNVRVSGWVEKLSINAVGEKVNKGDVLFTLYSPELVKAQDELISAYKTGRKG----LIK 191
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALskseLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 192 GSTERLITLGVDKTQIRSITRKGKASQTIEVKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWIS 271
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497531327 272 SGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
10-418 |
1.90e-65 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 219.35 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 10 ALLVGGALGFSVNHFVvGSAHNMSAMATSTGAEVskqtkdepLYWVAPMDPNYQRDKPGQSP-MGMDLIPVYADDvnGGA 88
Cdd:PRK09783 10 SMIAGGIISAAGFTWV-AKAEPPAEKTSTAERKV--------LFWYDPMYPNTRFDKPGKSPfMDMDLVPKYADE--ESS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 89 KDKPGtVFIDSFVENNLGVKTAQVTREALSPRIETVGYVAFDESALWQTNVRVSGWVEKLSINAVGEKVNKGDVLFTLYS 168
Cdd:PRK09783 79 ASSGG-VRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 169 PELVKAQDE-LISAYKTGRKGLIKGSTERLITLGVDKTQIRSI--TRKGKASQTIevKAPADGVIASLNIREGGYLSPAQ 245
Cdd:PRK09783 158 PDWVEAQSEyLLLRETGGTATQTEGILERLRLAGMPEADIRRLiaTRKIQTRFTL--KAPIDGVITAFDLRAGMNIAKDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 246 AVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:PRK09783 236 VVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 326 NIALKPISDEAVLtIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTSAHFMLDSESSQS 405
Cdd:PRK09783 316 WLQLNTASEPMLL-IPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANIS 394
|
410
....*....|...
gi 497531327 406 ADLSRINSVEEEA 418
Cdd:PRK09783 395 GALERMRSESATH 407
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
112-402 |
4.57e-60 |
|
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: 202.48 E-value: 4.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 112 VTREALSPRIETVGYVAFDESAlwqtNV--RVSGWVEKLSINaVGEKVNKGDVLFTLYSP----ELVKAQDELISAYKTG 185
Cdd:COG0845 3 VERGDVPETVEATGTVEARREV----EVraRVSGRVEEVLVD-EGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAQAQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 186 R---------KGLIKG---STERLIT----LGVDKTQIRS----ITRKGKASQTIEVKAPADGVIASLNIREGGYLSPAQ 245
Cdd:COG0845 78 ElakaeleryKALLKKgavSQQELDQakaaLDQAQAALAAaqaaLEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 246 AVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:COG0845 158 PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497531327 326 NIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTSAHFMLDSES 402
Cdd:COG0845 238 RVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGA 314
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
107-393 |
6.66e-34 |
|
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: 131.28 E-value: 6.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 107 VKTAQVTREALSPRIETVG-YVAFDESALwqtNVRVSGWVEKLSINAvGEKVNKGDVLFTLYSPEL-------------V 172
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGsLEAVDEADL---AAEVAGKITKISVRE-GQKVKKGQVLARLDDDDYqlalqaalaqlaaA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 173 KAQDELISAYKTGRKGLIKGSTERLITLGVDKTQIRS-ITRKGKASQTI----------EVKAPADGVIASLNIREGGYL 241
Cdd:TIGR01730 77 EAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAaQADLEAAKASLasaqlnlrytEIRAPFDGTIGRRLVEVGAYV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 242 SPAQAVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKP 321
Cdd:TIGR01730 157 TAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLP 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497531327 322 NMFANIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTS 393
Cdd:TIGR01730 237 GMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTA 308
|
|
| CusF_Ec |
pfam11604 |
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ... |
505-571 |
1.06e-19 |
|
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.
Pssm-ID: 463306 Cd Length: 68 Bit Score: 83.02 E-value: 1.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 505 GDITMLMADFGMITVKHQPVPEWNWKAGEMNFQASDDLDLSEFAEGQTIRFLVAKQGS-DYVLKSLEP 571
Cdd:pfam11604 1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPALLAGLKPGDKVRFEFEKDDGgEYTITKIEP 68
|
|
| CusF |
COG5569 |
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]; |
413-491 |
6.53e-19 |
|
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
Pssm-ID: 444311 Cd Length: 101 Bit Score: 81.96 E-value: 6.53e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497531327 413 SVEEEAETVWANGEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDFEMRKTESGRYEVVDYK 491
Cdd:COG5569 20 AAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPALLKGLKVGDKVRFEFERVGDGGYVITSIE 98
|
|
| CusF_Ec |
pfam11604 |
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ... |
425-489 |
3.49e-18 |
|
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.
Pssm-ID: 463306 Cd Length: 68 Bit Score: 78.78 E-value: 3.49e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497531327 425 GEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDFEMRKTESGRYEVVD 489
Cdd:pfam11604 1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPALLAGLKPGDKVRFEFEKDDGGEYTITK 65
|
|
| CusF |
COG5569 |
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]; |
501-573 |
5.01e-17 |
|
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
Pssm-ID: 444311 Cd Length: 101 Bit Score: 76.57 E-value: 5.01e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497531327 501 VWVTGDITMLMADFGMITVKHQPVPEWNWKAGEMNFQASDDLDLSEFAEGQTIRFLVAKQGS-DYVLKSLEPTN 573
Cdd:COG5569 28 AEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPALLKGLKVGDKVRFEFERVGDgGYVITSIEPAK 101
|
|
| PRK09838 |
PRK09838 |
periplasmic copper-binding protein; Provisional |
398-475 |
5.17e-07 |
|
periplasmic copper-binding protein; Provisional
Pssm-ID: 182104 Cd Length: 115 Bit Score: 48.71 E-value: 5.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 398 LDSESSQSADLSRiNSVEEEAETVWANGEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDF 475
Cdd:PRK09838 21 QANEHHQHGDMHE-AMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTITPQTKMSEIKTGDKVAF 97
|
|
| HMBD |
pfam19335 |
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ... |
53-79 |
5.71e-07 |
|
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: 46.05 E-value: 5.71e-07
10 20
....*....|....*....|....*...
gi 497531327 53 YWVAPMDPNYQRDKPGQSP-MGMDLIPV 79
Cdd:pfam19335 1 KYICPMHPDITSDKPGKCPiCGMALVPV 28
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
300-420 |
9.55e-07 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 51.33 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 300 DPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIE 379
Cdd:PRK09578 267 DPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWI 346
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 497531327 380 VLQGLEQGENIVTsahfmldSESSQSADLSRINSVEEEAET 420
Cdd:PRK09578 347 VTRGLAGGERVIV-------DNAAQFAPGTAVKAVERAPAA 380
|
|
| |
|
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 ... |
116-325 |
5.36e-95 |
|
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: 289.41 E-value: 5.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 116 ALSPRIETVGYVAFDESALWQTNVRVSGWVEKLSINAVGEKVNKGDVLFTLYSPELVKAQDELISAYKTGRKG----LIK 191
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALskseLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 192 GSTERLITLGVDKTQIRSITRKGKASQTIEVKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWIS 271
Cdd:pfam16576 81 AARQRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497531327 272 SGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:pfam16576 161 VGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
10-418 |
1.90e-65 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 219.35 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 10 ALLVGGALGFSVNHFVvGSAHNMSAMATSTGAEVskqtkdepLYWVAPMDPNYQRDKPGQSP-MGMDLIPVYADDvnGGA 88
Cdd:PRK09783 10 SMIAGGIISAAGFTWV-AKAEPPAEKTSTAERKV--------LFWYDPMYPNTRFDKPGKSPfMDMDLVPKYADE--ESS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 89 KDKPGtVFIDSFVENNLGVKTAQVTREALSPRIETVGYVAFDESALWQTNVRVSGWVEKLSINAVGEKVNKGDVLFTLYS 168
Cdd:PRK09783 79 ASSGG-VRIDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 169 PELVKAQDE-LISAYKTGRKGLIKGSTERLITLGVDKTQIRSI--TRKGKASQTIevKAPADGVIASLNIREGGYLSPAQ 245
Cdd:PRK09783 158 PDWVEAQSEyLLLRETGGTATQTEGILERLRLAGMPEADIRRLiaTRKIQTRFTL--KAPIDGVITAFDLRAGMNIAKDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 246 AVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:PRK09783 236 VVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 326 NIALKPISDEAVLtIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTSAHFMLDSESSQS 405
Cdd:PRK09783 316 WLQLNTASEPMLL-IPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANIS 394
|
410
....*....|...
gi 497531327 406 ADLSRINSVEEEA 418
Cdd:PRK09783 395 GALERMRSESATH 407
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
112-402 |
4.57e-60 |
|
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: 202.48 E-value: 4.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 112 VTREALSPRIETVGYVAFDESAlwqtNV--RVSGWVEKLSINaVGEKVNKGDVLFTLYSP----ELVKAQDELISAYKTG 185
Cdd:COG0845 3 VERGDVPETVEATGTVEARREV----EVraRVSGRVEEVLVD-EGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAQAQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 186 R---------KGLIKG---STERLIT----LGVDKTQIRS----ITRKGKASQTIEVKAPADGVIASLNIREGGYLSPAQ 245
Cdd:COG0845 78 ElakaeleryKALLKKgavSQQELDQakaaLDQAQAALAAaqaaLEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 246 AVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFA 325
Cdd:COG0845 158 PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497531327 326 NIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTSAHFMLDSES 402
Cdd:COG0845 238 RVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGA 314
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
107-393 |
6.66e-34 |
|
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: 131.28 E-value: 6.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 107 VKTAQVTREALSPRIETVG-YVAFDESALwqtNVRVSGWVEKLSINAvGEKVNKGDVLFTLYSPEL-------------V 172
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGsLEAVDEADL---AAEVAGKITKISVRE-GQKVKKGQVLARLDDDDYqlalqaalaqlaaA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 173 KAQDELISAYKTGRKGLIKGSTERLITLGVDKTQIRS-ITRKGKASQTI----------EVKAPADGVIASLNIREGGYL 241
Cdd:TIGR01730 77 EAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAaQADLEAAKASLasaqlnlrytEIRAPFDGTIGRRLVEVGAYV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 242 SPAQAVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKP 321
Cdd:TIGR01730 157 TAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLP 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497531327 322 NMFANIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTS 393
Cdd:TIGR01730 237 GMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTA 308
|
|
| CusF_Ec |
pfam11604 |
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ... |
505-571 |
1.06e-19 |
|
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.
Pssm-ID: 463306 Cd Length: 68 Bit Score: 83.02 E-value: 1.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 505 GDITMLMADFGMITVKHQPVPEWNWKAGEMNFQASDDLDLSEFAEGQTIRFLVAKQGS-DYVLKSLEP 571
Cdd:pfam11604 1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPALLAGLKPGDKVRFEFEKDDGgEYTITKIEP 68
|
|
| CusF |
COG5569 |
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]; |
413-491 |
6.53e-19 |
|
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
Pssm-ID: 444311 Cd Length: 101 Bit Score: 81.96 E-value: 6.53e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497531327 413 SVEEEAETVWANGEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDFEMRKTESGRYEVVDYK 491
Cdd:COG5569 20 AAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPALLKGLKVGDKVRFEFERVGDGGYVITSIE 98
|
|
| CusF_Ec |
pfam11604 |
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ... |
425-489 |
3.49e-18 |
|
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.
Pssm-ID: 463306 Cd Length: 68 Bit Score: 78.78 E-value: 3.49e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497531327 425 GEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDFEMRKTESGRYEVVD 489
Cdd:pfam11604 1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPALLAGLKPGDKVRFEFEKDDGGEYTITK 65
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
105-331 |
5.68e-18 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 85.10 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 105 LGVKTAQVTREALSPRIETVGYVAFDESALwqtNVRVSGWVEKLSINaVGEKVNKGDVLFTLYSPEL------------- 171
Cdd:COG1566 19 LGLALWAAGRNGPDEPVTADGRVEARVVTV---AAKVSGRVTEVLVK-EGDRVKKGQVLARLDPTDLqaalaqaeaqlaa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 172 -----------------VKAQDELISAYKTG---------------RKGLIkgSTERL------------------ITLG 201
Cdd:COG1566 95 aeaqlarleaelgaeaeIAAAEAQLAAAQAQldlaqreleryqalyKKGAV--SQQELdearaaldaaqaqleaaqAQLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 202 VDKTQIRSITRKGKASQTIE-----------------VKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFE 264
Cdd:COG1566 173 QAQAGLREEEELAAAQAQVAqaeaalaqaelnlarttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPE 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 265 RQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKT----------RTLRVRLKFSNPNGE-LKPNMFANIALKP 331
Cdd:COG1566 253 TDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSppknatgnvvQRYPVRIRLDNPDPEpLRPGMSATVEIDT 330
|
|
| CusF |
COG5569 |
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism]; |
501-573 |
5.01e-17 |
|
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
Pssm-ID: 444311 Cd Length: 101 Bit Score: 76.57 E-value: 5.01e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497531327 501 VWVTGDITMLMADFGMITVKHQPVPEWNWKAGEMNFQASDDLDLSEFAEGQTIRFLVAKQGS-DYVLKSLEPTN 573
Cdd:COG5569 28 AEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPALLKGLKVGDKVRFEFERVGDgGYVITSIEPAK 101
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
221-320 |
1.52e-16 |
|
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: 75.48 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 221 EVKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILD 300
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|
gi 497531327 301 PKTRTLRVRLKFSNPNGELK 320
Cdd:pfam13437 81 PDTGVIPVRVSIENPKTPIP 100
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
154-394 |
1.24e-10 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 63.58 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 154 GEKVNKGDVLFTLySPELVKAqdELISAYKTGRKGLIKGSTERLI------------TLGVDKTQIRSITRKGKASQTIe 221
Cdd:PRK09859 80 GDKVNQGDSLYQI-DPAPLQA--ELNSAKGSLAKALSTASNARITfnrqasllktnyVSRQDYDTARTQLNEAEANVTV- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 222 vkAPADGVIASLNIREGGYLSP--------------------AQAVISAGPLGEVWVD----AEVFERQAHWISSGS--- 274
Cdd:PRK09859 156 --AKAAVEQATINLQYANVTSPitgvsgkssvtvgalvtanqADSLVTVQRLDPIYVDltqsVQDFLRMKEEVASGQikq 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 275 ---NAVMTLDAIPGKEW--LGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVIHSG 349
Cdd:PRK09859 234 vqgSTPVQLNLENGKRYsqTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNA 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 497531327 350 -GMTRVVMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTSA 394
Cdd:PRK09859 314 qGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
|
|
| PRK09838 |
PRK09838 |
periplasmic copper-binding protein; Provisional |
398-475 |
5.17e-07 |
|
periplasmic copper-binding protein; Provisional
Pssm-ID: 182104 Cd Length: 115 Bit Score: 48.71 E-value: 5.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497531327 398 LDSESSQSADLSRiNSVEEEAETVWANGEISDVMQGSRMVMINHQPVPEWDWPGMVMNFTFAEGLDMSDVERGKAIDF 475
Cdd:PRK09838 21 QANEHHQHGDMHE-AMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTITPQTKMSEIKTGDKVAF 97
|
|
| HMBD |
pfam19335 |
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ... |
53-79 |
5.71e-07 |
|
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: 46.05 E-value: 5.71e-07
10 20
....*....|....*....|....*...
gi 497531327 53 YWVAPMDPNYQRDKPGQSP-MGMDLIPV 79
Cdd:pfam19335 1 KYICPMHPDITSDKPGKCPiCGMALVPV 28
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
300-420 |
9.55e-07 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 51.33 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 300 DPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVIHSGGMTRVVMSEGSGKYRSARIEVGREAGEKIE 379
Cdd:PRK09578 267 DPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWI 346
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 497531327 380 VLQGLEQGENIVTsahfmldSESSQSADLSRINSVEEEAET 420
Cdd:PRK09578 347 VTRGLAGGERVIV-------DNAAQFAPGTAVKAVERAPAA 380
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
140-393 |
1.31e-06 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 50.93 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 140 RVSGWVEKLSInAVGEKVNKGDVLfTLYSPE-------------------LVKAQDELISAYKT-------------GRK 187
Cdd:PRK11578 67 QVSGQLKTLSV-AIGDKVKKDQLL-GVIDPEqaenqikeveatlmelraqRQQAEAELKLARVTlsrqqrlaktqavSQQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 188 GLIKGSTErlitLGVDKTQIRSI---TRKGKAS--------QTIEVKAPADGVIASLNIREGGYLSPAQA---VISAGPL 253
Cdd:PRK11578 145 DLDTAATE----LAVKQAQIGTIdaqIKRNQASldtaktnlDYTRIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADM 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 254 GEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYVYPILDPKTRTL--RVRLKFSNPNGELKPNMFANIALKP 331
Cdd:PRK11578 221 STMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIfyYARFEVPNPNGLLRLDMTAQVHIQL 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497531327 332 ISDEAVLTIPRSSVIHSGGMTRV-VMSEGSGKYRSARIEVGREAGEKIEVLQGLEQGENIVTS 393
Cdd:PRK11578 301 TDVKNVLTIPLSALGDPVGDNRYkVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIG 363
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
218-286 |
5.11e-05 |
|
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: 45.49 E-value: 5.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 218 QTIEVKAPADGVIASLNIR-EGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGK 286
Cdd:pfam00529 208 ERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQT 277
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
221-394 |
5.17e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 45.86 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 221 EVKAPADGVIASLNIREGGYLSPAQA--VISAGPLGEVWVD----AEVFERQAHWISSGS---------NAVMTLDAIPG 285
Cdd:PRK15030 175 KVTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPIYVDvtqsSNDFLRLKQELANGTlkqengkakVSLITSDGIKF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 286 KEwLGNVDYVYPILDPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVIHSG-GMTRVVMSEGSGKYR 364
Cdd:PRK15030 255 PQ-DGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPrGDATVLVVGADDKVE 333
|
170 180 190
....*....|....*....|....*....|
gi 497531327 365 SARIEVGREAGEKIEVLQGLEQGENIVTSA 394
Cdd:PRK15030 334 TRPIVASQAIGDKWLVTEGLKAGDRVVISG 363
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
299-392 |
2.78e-04 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 43.63 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 299 LDPKTRTLRVRLKFSNPNGELKPNMFANIALKPISDEAVLTIPRSSVI--HSGGMTRVVMSEgsGKYRSARIEVGREAGE 376
Cdd:PRK11556 283 IDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQmgNEGHFVWVLNDE--NKVSKHLVTPGIQDSQ 360
|
90
....*....|....*.
gi 497531327 377 KIEVLQGLEQGENIVT 392
Cdd:PRK11556 361 KVVISAGLSAGDRVVT 376
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
216-323 |
9.55e-04 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 41.49 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531327 216 ASQTIEVKAPADGVIASLNIREGGYLSPAQAVISAGPLGEVWVDAEVFERQAHWISSGSNAVMTLDAIPGKEWLGNVDYV 295
Cdd:PRK03598 200 NLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFV 279
|
90 100 110
....*....|....*....|....*....|....*....
gi 497531327 296 YPILD--PKT------RT---LRVRLKFSNPNGELKPNM 323
Cdd:PRK03598 280 SPTAEftPKTvetpdlRTdlvYRLRIVVTDADDALRQGM 318
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