|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
41-455 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 804.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 41 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRAGPLAPVQAATAVEQAVPRYLTGLG 120
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 121 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 200
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 201 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 280
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 281 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 360
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 361 AVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTSE 440
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 349738460 441 EKATSREYAKKGARS 455
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
106-436 |
9.27e-108 |
|
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: 321.89 E-value: 9.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 106 TAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 185
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 186 RDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 265
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 266 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 345
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 346 NQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 425
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 349738460 426 AKVEVVEAQSA 436
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
102-431 |
1.12e-78 |
|
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: 247.23 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 102 VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 181
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 182 ANARRDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 261
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 262 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 341
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 342 ALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 421
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 349738460 422 LTEGAKVEVV 431
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
121-416 |
9.73e-34 |
|
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: 129.08 E-value: 9.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 121 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 200
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 201 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 280
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 281 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 348
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 349738460 349 VNARMLVDTEQNAVVIPTAALQMGNEGHF-VWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 416
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
129-158 |
3.68e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 38.55 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|
gi 349738460 129 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 158
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
41-455 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 804.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 41 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRAGPLAPVQAATAVEQAVPRYLTGLG 120
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 121 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 200
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 201 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 280
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 281 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 360
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 361 AVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTSE 440
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 349738460 441 EKATSREYAKKGARS 455
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
106-436 |
9.27e-108 |
|
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: 321.89 E-value: 9.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 106 TAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 185
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 186 RDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 265
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 266 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 345
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 346 NQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 425
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 349738460 426 AKVEVVEAQSA 436
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
102-431 |
1.12e-78 |
|
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: 247.23 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 102 VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 181
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 182 ANARRDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 261
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 262 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 341
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 342 ALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 421
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 349738460 422 LTEGAKVEVV 431
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
90-437 |
2.91e-42 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 153.80 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 90 GRRGMRAGPLAP--VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVAL 167
Cdd:PRK09578 24 GKGDSDAAAAAPreATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 168 AQAQGQLAKDKATLANARRDLARYQQLVKTNLVSrqELDAQQALVSETEGtiKADEAS----VASAQLQLDWSRITAPVD 243
Cdd:PRK09578 104 DAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVS--ERDYTEAVADERQA--KAAVASakaeLARAQLQLDYATVTAPID 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 244 GRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGT-------L 316
Cdd:PRK09578 180 GRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSeyplkgkL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 317 LSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSK-HLVTPG 395
Cdd:PRK09578 260 LFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDvEVEADQ 339
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 349738460 396 IQDSQKVVIRaGISAGDRVVTDGIDRLTEGAKVEVVEAQSAT 437
Cdd:PRK09578 340 MSGRDWIVTR-GLAGGERVIVDNAAQFAPGTAVKAVERAPAA 380
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
81-446 |
1.76e-41 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 152.18 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 81 KQAQQspaGGRRGMRAGPLAPVQAATAVEQAVPryltglGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDP 160
Cdd:PRK15030 28 KQAQQ---GGQQMPAVGVVTVKTEPLQITTELP------GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 161 SQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITA 240
Cdd:PRK15030 99 ATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 241 PVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVVQ-------AQKAGKPlVVEAWDRTNSKKLSE 313
Cdd:PRK15030 179 PISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQelangtlKQENGKA-KVSLITSDGIKFPQD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 314 GTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGH-FVWVLNSENKVSKHLV 392
Cdd:PRK15030 258 GTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETRPI 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 349738460 393 TPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEA-----QSATTSEEKATSR 446
Cdd:PRK15030 338 VASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVtadnnQQAASGAQPEQSK 396
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
130-441 |
2.35e-40 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 148.71 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 130 VRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLVSRQELDAQQ 209
Cdd:PRK09859 64 IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTAR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 210 ALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVV 289
Cdd:PRK09859 144 TQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 290 QAQKAGKPLVVE-----AWDRTNSKKLSE-GTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVV 363
Cdd:PRK09859 224 EEVASGQIKQVQgstpvQLNLENGKRYSQtGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLL 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 349738460 364 IPTAALQMGNEGHFV-WVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTSEE 441
Cdd:PRK09859 304 VPQEGVTHNAQGKATaLILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTE 382
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
121-416 |
9.73e-34 |
|
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: 129.08 E-value: 9.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 121 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 200
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 201 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 280
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 281 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 348
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 349738460 349 VNARMLVDTEQNAVVIPTAALQMGNEGHF-VWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 416
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
110-358 |
9.09e-33 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 126.70 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 110 QAVPRYLTGLGTITAaNTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA-------------- 175
Cdd:COG1566 29 NGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 176 -------------KDKATLANARRDLARYQQLVKTNLVSRQELDAQQALVSETEGTIKAD-------------------- 222
Cdd:COG1566 108 aeaeiaaaeaqlaAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeeelaaa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 223 -------EASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVVQAQKAg 295
Cdd:COG1566 188 qaqvaqaEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDLGRVKPGQPV- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349738460 296 kPLVVEAWDrtnSKKLsEGTLLSLDNQIDATTG----------TIKVKARFNNQD-DALFPNQFVNARmlVDTE 358
Cdd:COG1566 265 -EVRVDAYP---DRVF-EGKVTSISPGAGFTSPpknatgnvvqRYPVRIRLDNPDpEPLRPGMSATVE--IDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
97-416 |
7.78e-23 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 99.46 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 97 GPLAPVQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFK-------VALAQ 169
Cdd:PRK11578 31 APVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLME 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 170 AQGQLAKDKATLANARRDLARYQQLVKTNLVSRQELD-------AQQALVSETEGTIKADEASVASAQLQLDWSRITAPV 242
Cdd:PRK11578 111 LRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDtaatelaVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 243 DGRVglkqvdvgNQISS--GDTtgiVVITQTHPIDLlfTLpeSDIAT-VVQAQkagkplVVEAwDRTNSKKLSEGTLLSL 319
Cdd:PRK11578 191 AGEV--------TQITTlqGQT---VIAAQQAPNIL--TL--ADMSTmLVKAQ------VSEA-DVIHLKPGQKAWFTVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 320 DNQIDATTGTIK-VKARFNNQDDALF---------PNQFVNARM------LVDTEQNAVVIPTAAL--QMGNEGHFVWVL 381
Cdd:PRK11578 249 GDPLTRYEGVLKdILPTPEKVNDAIFyyarfevpnPNGLLRLDMtaqvhiQLTDVKNVLTIPLSALgdPVGDNRYKVKLL 328
|
330 340 350
....*....|....*....|....*....|....*
gi 349738460 382 NsENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 416
Cdd:PRK11578 329 R-NGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
127-274 |
7.23e-16 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 78.47 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 127 TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLA------------------------ 182
Cdd:PRK03598 43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkqaqaa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 183 --NARRDLARYQQLVKTNLVSRQELD---------------AQQAL-----------VSETEGTIKADEASVASAQLQLD 234
Cdd:PRK03598 123 ydYAQNFYNRQQGLWKSRTISANDLEnarssrdqaqatlksAQDKLsqyregnrpqdIAQAKASLAQAQAALAQAELNLQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 349738460 235 WSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPI 274
Cdd:PRK03598 203 DTELIAPSDGTILTRAVEPGTMLNAGST--VFTLSLTRPV 240
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
125-284 |
2.04e-15 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 77.37 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 125 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARR------------------ 186
Cdd:PRK10476 46 ADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRsvdaersnaasaneqver 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 187 ----------DLARYQQLVKTNLVSRQELD---------------------AQQALVSET---EGTIKADEASVASAQLQ 232
Cdd:PRK10476 126 aranaklatrTLERLEPLLAKGYVSAQQVDqartaqrdaevslnqallqaqAAAAAVGGVdalVAQRAAREAALAIAELH 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 349738460 233 LDWSRITAPVDGRVglkqvdVGNQISSGDTTGivvitqthPIDLLFTLPESD 284
Cdd:PRK10476 206 LEDTTVRAPFDGRV------VGLKVSVGEFAA--------PMQPIFTLIDTD 243
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
126-175 |
2.53e-12 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 61.30 E-value: 2.53e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 349738460 126 NTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA 175
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
124-288 |
2.70e-11 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 64.38 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 124 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLvKTNLVSRQ 203
Cdd:PRK10559 44 SADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 204 ELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTgiVVITQTHPIDLLFTLPES 283
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA--VALVKQNSFYVLAYMEET 200
|
....*
gi 349738460 284 DIATV 288
Cdd:PRK10559 201 KLEGV 205
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
124-260 |
2.75e-11 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 65.10 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 124 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKD---------------------KATLA 182
Cdd:PRK15136 58 AGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyqanielqKTALA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 183 NARRDLARYQQLVKTNLVSRQEL---------------------DAQQALVSET----EGTIKADEASVASAQLQLDWSR 237
Cdd:PRK15136 138 QAQSDLNRRVPLGNANLIGREELqhardavasaqaqldvaiqqyNANQAMILNTpledQPAVQQAATEVRNAWLALQRTK 217
|
170 180
....*....|....*....|...
gi 349738460 238 ITAPVDGRVGLKQVDVGNQISSG 260
Cdd:PRK15136 218 IVSPMTGYVSRRSVQVGAQISPT 240
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
238-419 |
3.37e-07 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 52.18 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 238 ITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESdIATVVQAQKAGKpLVVEAWDRTnSKKLSEGTLL 317
Cdd:PRK09783 212 LKAPIDGVITAFDLRAGMNIAKDNV--VAKIQGMDPVWVTAAIPES-IAWLVKDASQFT-LTVPARPDK-TFTIRKWTLL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 318 SldnQIDATTGTIKVKARFNNQDDALFPNqfVNARMLVDTE-QNAVVIPTAAL-QMGNEGHFVWVLNSENKVSKHLVTpg 395
Cdd:PRK09783 287 P---SVDAATRTLQLRLEVDNADEALKPG--MNAWLQLNTAsEPMLLIPSQALiDTGSEQRVITVDADGRFVPKRVAV-- 359
|
170 180
....*....|....*....|....*
gi 349738460 396 IQDSQKVV-IRAGISAGDRVVTDGI 419
Cdd:PRK09783 360 FQESQGVTaIRSGLAEGEKVVSSGL 384
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
114-349 |
2.38e-06 |
|
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: 48.27 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 114 RYLTGLGTITA--ANTVTVRSRVDGQLMALHFQ-EGQQVKAGDLLAEIDPSQfkvaLAQAQGQLAkdkatLANARRDLAR 190
Cdd:pfam16576 4 RTIRAVGRVAYdeRRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEYL-----LALRSGDALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 191 YQQLVKTnlvSRQELdaqqALVSETEGTIKADEASVASAQlqldWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQ 270
Cdd:pfam16576 75 KSELLRA---ARQRL----RLLGMPEAQIAELERTGKVQP----TVTVYAPISGVVTELNVREGMYVQPGDT--LFTIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 271 THPIDLLFTLPESDIATVvqaqKAGKPLVV-------EAWdrtnskklsEGTLLSLDNQIDATTGTIKVKARFNNQDDAL 343
Cdd:pfam16576 142 LSTVWVEADVPEQDLALV----KVGQPAEVtlpalpgKTF---------EGKVDYIYPTLDPKTRTVRVRIELPNPDGRL 208
|
....*.
gi 349738460 344 FPNQFV 349
Cdd:pfam16576 209 KPGMFA 214
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
122-192 |
1.52e-04 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 43.84 E-value: 1.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349738460 122 ITAANTVTVRSRVD-------GQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQlakdkatLANARRDLARYQ 192
Cdd:TIGR01843 31 ATATGKVVPSGNVKvvqhlegGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQ-------VLRLEAEVARLR 101
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
237-343 |
3.22e-04 |
|
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: 40.04 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349738460 237 RITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTL 316
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP--LATIVPPDRLLVEAFVPAADLGSL----KKGQKVTLKL--DPGSDYTLEGKV 72
|
90 100
....*....|....*....|....*..
gi 349738460 317 LSLDNQIDATTGTIKVKARFNNQDDAL 343
Cdd:pfam13437 73 VRISPTVDPDTGVIPVRVSIENPKTPI 99
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
129-158 |
3.68e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 38.55 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|
gi 349738460 129 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 158
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
129-179 |
1.41e-03 |
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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: 38.11 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 349738460 129 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI-DPSQFKVALAQAQGQLAKDKA 179
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEAFVPAADLGSLKK 52
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| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
129-160 |
3.92e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.74 E-value: 3.92e-03
10 20 30
....*....|....*....|....*....|..
gi 349738460 129 TVRSRVDGQLMALHFQEGQQVKAGDLLAEIDP 160
Cdd:PRK12999 1115 TITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
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| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
129-158 |
4.08e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 39.68 E-value: 4.08e-03
10 20 30
....*....|....*....|....*....|
gi 349738460 129 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 158
Cdd:COG1038 1115 TITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
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