|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
1-415 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 783.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 1 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRSGPLAPVQAVTAVEQAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 81 TIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 321 AVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPE 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 446601663 401 EKATSREYAKKGARS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-396 |
1.20e-104 |
|
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: 312.65 E-value: 1.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 66 TAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 146 RDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 226 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 306 NQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 446601663 386 AKVEVVEAQSA 396
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
1.89e-76 |
|
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: 240.29 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 62 VQAVTAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 142 ANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 222 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 302 ALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 446601663 382 LTEGAKVEVV 391
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 ... |
81-376 |
5.78e-33 |
|
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: 126.38 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 81 TIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 241 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446601663 309 VNARMLVDTEQNAVVIPTAALQMGNEGHF-VWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
89-118 |
2.41e-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: 38.94 E-value: 2.41e-04
10 20 30
....*....|....*....|....*....|
gi 446601663 89 TVRSRVDGQLIALHFQEGQQVKAGDLLAEI 118
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
1-415 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 783.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 1 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRSGPLAPVQAVTAVEQAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 81 TIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 321 AVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPE 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 446601663 401 EKATSREYAKKGARS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-396 |
1.20e-104 |
|
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: 312.65 E-value: 1.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 66 TAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 146 RDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 226 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 306 NQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 446601663 386 AKVEVVEAQSA 396
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
1.89e-76 |
|
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: 240.29 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 62 VQAVTAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 142 ANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 222 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 302 ALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 446601663 382 LTEGAKVEVV 391
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
62-399 |
7.91e-41 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 149.17 E-value: 7.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 62 VQAVTAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:PRK09578 38 ATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 142 ANARRDLARYQQLAKTNLVSrqELDAQQALVSETEGtiKADEAS----VASAQLQLDWSRITAPVDGRVGLKQVDVGNQI 217
Cdd:PRK09578 118 LAALDKRRRYDDLVRDRAVS--ERDYTEAVADERQA--KAAVASakaeLARAQLQLDYATVTAPIDGRARRALVTEGALV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 218 SSGDTTGIVVITQTHPIDLLFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGT-------LLSLDNQIDATTGTI 290
Cdd:PRK09578 194 GQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSeyplkgkLLFSDLAVDPTTDTV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 291 KVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLSSENKVSK-HLVTPGIQDSQKVVIRaGIS 369
Cdd:PRK09578 274 AMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDvEVEADQMSGRDWIVTR-GLA 352
|
330 340 350
....*....|....*....|....*....|
gi 446601663 370 AGDRVVTDGIDRLTEGAKVEVVEAQSATTP 399
Cdd:PRK09578 353 GGERVIVDNAAQFAPGTAVKAVERAPAAKP 382
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
39-401 |
4.58e-40 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 147.17 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 39 ATKQAQQSPAGGRRGMRSGPLapvQAVTAVEqavpryltglGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEI 118
Cdd:PRK15030 30 AQQGGQQMPAVGVVTVKTEPL---QITTELP----------GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 119 DPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRI 198
Cdd:PRK15030 97 DPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 199 TAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVVQ-------AQKAGKPlVVEAWDRTNSKKL 271
Cdd:PRK15030 177 TSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQelangtlKQENGKA-KVSLITSDGIKFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 272 SEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGH-FVWVLSSENKVSKH 350
Cdd:PRK15030 256 QDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETR 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446601663 351 LVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVE--------AQSATTPEE 401
Cdd:PRK15030 336 PIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEvtadnnqqAASGAQPEQ 394
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
80-402 |
2.50e-39 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 144.86 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 80 GTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNL 159
Cdd:PRK09859 54 GRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 160 VSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFT 239
Cdd:PRK09859 134 VSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 240 LPESDIATVVQAQKAGKPLVVE-----AWDRTNSKKLSE-GTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARM 313
Cdd:PRK09859 214 QSVQDFLRMKEEVASGQIKQVQgstpvQLNLENGKRYSQtGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 314 LVDTEQNAVVIPTAALQMGNEGHFV-WVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVE 392
Cdd:PRK09859 294 DEGSRQNVLLVPQEGVTHNAQGKATaLILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAIS 373
|
330
....*....|..
gi 446601663 393 A--QSATTPEEK 402
Cdd:PRK09859 374 SsqENASTESKQ 385
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
81-376 |
5.78e-33 |
|
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: 126.38 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 81 TIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 241 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446601663 309 VNARMLVDTEQNAVVIPTAALQMGNEGHF-VWVLSSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
70-316 |
2.99e-31 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 121.69 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 70 QAVPRYLTGLGTIiAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA-------------- 135
Cdd:COG1566 29 NGPDEPVTADGRV-EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 136 -------------KDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKAD-------------------- 182
Cdd:COG1566 108 aeaeiaaaeaqlaAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeeelaaa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 183 -------EASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVVQAQKAg 255
Cdd:COG1566 188 qaqvaqaEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDLGRVKPGQPV- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446601663 256 kPLVVEAWDrtnSKKLsEGTLLSLDNQIDATTG----------TIKVKARFNNQD-DALFPNQFVNARMLVD 316
Cdd:COG1566 265 -EVRVDAYP---DRVF-EGKVTSISPGAGFTSPpknatgnvvqRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
56-376 |
2.18e-22 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 97.54 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 56 SGPLAPVQAVTAVEQAVPRYLTGLGTIIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFK-------VALA 128
Cdd:PRK11578 30 NAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 129 QAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELD-------AQQALVSETEGTIKADEASVASAQLQLDWSRITAP 201
Cdd:PRK11578 110 ELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDtaatelaVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 202 VDGRVglkqvdvgNQISS--GDTtgiVVITQTHPIDLLFT----------LPESDIATVVQAQKA-----GKPLvveawd 264
Cdd:PRK11578 190 MAGEV--------TQITTlqGQT---VIAAQQAPNILTLAdmstmlvkaqVSEADVIHLKPGQKAwftvlGDPL------ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 265 rtnskKLSEGTLLSLDNQIDATTGTIKVKARFN--NQDDALFPNQFVNARMLVDTEQNAVVIPTAAL--QMGNEGHFVWV 340
Cdd:PRK11578 253 -----TRYEGVLKDILPTPEKVNDAIFYYARFEvpNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALgdPVGDNRYKVKL 327
|
330 340 350
....*....|....*....|....*....|....*.
gi 446601663 341 LsSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:PRK11578 328 L-RNGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
82-244 |
4.53e-16 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 78.92 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 82 IIAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARR--------------- 146
Cdd:PRK10476 43 YIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRsvdaersnaasaneq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 147 -------------DLARYQQLAKTNLVSRQELD---------------------AQQALVSET---EGTIKADEASVASA 189
Cdd:PRK10476 123 veraranaklatrTLERLEPLLAKGYVSAQQVDqartaqrdaevslnqallqaqAAAAAVGGVdalVAQRAAREAALAIA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446601663 190 QLQLDWSRITAPVDGRVglkqvdVGNQISSGDTTGivvitqthPIDLLFTLPESD 244
Cdd:PRK10476 203 ELHLEDTTVRAPFDGRV------VGLKVSVGEFAA--------PMQPIFTLIDTD 243
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
87-234 |
6.45e-15 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 75.38 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 87 TVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLA------------------------ 142
Cdd:PRK03598 43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkqaqaa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 143 --NARRDLARYQQLAKTNLVSRQELD---------------AQQAL-----------VSETEGTIKADEASVASAQLQLD 194
Cdd:PRK03598 123 ydYAQNFYNRQQGLWKSRTISANDLEnarssrdqaqatlksAQDKLsqyregnrpqdIAQAKASLAQAQAALAQAELNLQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446601663 195 WSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPI 234
Cdd:PRK03598 203 DTELIAPSDGTILTRAVEPGTMLNAGST--VFTLSLTRPV 240
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
83-220 |
5.81e-12 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 66.64 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 83 IAANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKD---------------------KATL 141
Cdd:PRK15136 57 VAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyqanielqKTAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 142 ANARRDLARYQQLAKTNLVSRQEL---------------------DAQQALVSET----EGTIKADEASVASAQLQLDWS 196
Cdd:PRK15136 137 AQAQSDLNRRVPLGNANLIGREELqhardavasaqaqldvaiqqyNANQAMILNTpledQPAVQQAATEVRNAWLALQRT 216
|
170 180
....*....|....*....|....
gi 446601663 197 RITAPVDGRVGLKQVDVGNQISSG 220
Cdd:PRK15136 217 KIVSPMTGYVSRRSVQVGAQISPT 240
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
86-135 |
2.28e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 58.61 E-value: 2.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446601663 86 NTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA 135
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
84-248 |
2.36e-11 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 64.38 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 84 AANTVTVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAkTNLVSRQ 163
Cdd:PRK10559 44 SADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLG-VQAMSRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 164 ELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTgiVVITQTHPIDLLFTLPES 243
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA--VALVKQNSFYVLAYMEET 200
|
....*
gi 446601663 244 DIATV 248
Cdd:PRK10559 201 KLEGV 205
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
198-379 |
1.10e-06 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 50.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 198 ITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESdIATVVQAQKAGKpLVVEAWDRTnSKKLSEGTLL 277
Cdd:PRK09783 212 LKAPIDGVITAFDLRAGMNIAKDNV--VAKIQGMDPVWVTAAIPES-IAWLVKDASQFT-LTVPARPDK-TFTIRKWTLL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 278 SldnQIDATTGTIKVKARFNNQDDALFPNqfVNARMLVDTE-QNAVVIPTAAL-QMGNEGHFVWVLSSENKVSKHLVTpg 355
Cdd:PRK09783 287 P---SVDAATRTLQLRLEVDNADEALKPG--MNAWLQLNTAsEPMLLIPSQALiDTGSEQRVITVDADGRFVPKRVAV-- 359
|
170 180
....*....|....*....|....*
gi 446601663 356 IQDSQKVV-IRAGISAGDRVVTDGI 379
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 ... |
87-309 |
5.71e-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: 47.12 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 87 TVTVRSRVDGQLIALHFQ-EGQQVKAGDLLAEIDPSQfkvaLAQAQGQLAkdkatLANARRDLARYQQLAKTnlvSRQEL 165
Cdd:pfam16576 19 LAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEYL-----LALRSGDALSKSELLRA---ARQRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 166 daqqALVSETEGTIKADEASVASAQlqldWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDI 245
Cdd:pfam16576 87 ----RLLGMPEAQIAELERTGKVQP----TVTVYAPISGVVTELNVREGMYVQPGDT--LFTIADLSTVWVEADVPEQDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446601663 246 ATVvqaqKAGKPLVV-------EAWdrtnskklsEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFV 309
Cdd:pfam16576 157 ALV----KVGQPAEVtlpalpgKTF---------EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
77-156 |
1.87e-05 |
|
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: 46.54 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 77 TGLGTIIAANTV-TVRSRVDGQLIALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQlakdkatLANARRDLARYQQLA 155
Cdd:TIGR01843 32 TATGKVVPSGNVkVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQ-------VLRLEAEVARLRAEA 104
|
.
gi 446601663 156 K 156
Cdd:TIGR01843 105 D 105
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
89-118 |
2.41e-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: 38.94 E-value: 2.41e-04
10 20 30
....*....|....*....|....*....|
gi 446601663 89 TVRSRVDGQLIALHFQEGQQVKAGDLLAEI 118
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
197-303 |
8.54e-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: 38.50 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601663 197 RITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTL 276
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP--LATIVPPDRLLVEAFVPAADLGSL----KKGQKVTLKL--DPGSDYTLEGKV 72
|
90 100
....*....|....*....|....*..
gi 446601663 277 LSLDNQIDATTGTIKVKARFNNQDDAL 303
Cdd:pfam13437 73 VRISPTVDPDTGVIPVRVSIENPKTPI 99
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
89-120 |
4.81e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.35 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|..
gi 446601663 89 TVRSRVDGQLIALHFQEGQQVKAGDLLAEIDP 120
Cdd:PRK12999 1115 TITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
89-139 |
4.87e-03 |
|
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: 36.57 E-value: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446601663 89 TVRSRVDGQLIALHFQEGQQVKAGDLLAEI-DPSQFKVALAQAQGQLAKDKA 139
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEAFVPAADLGSLKK 52
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
89-118 |
5.05e-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: 39.29 E-value: 5.05e-03
10 20 30
....*....|....*....|....*....|
gi 446601663 89 TVRSRVDGQLIALHFQEGQQVKAGDLLAEI 118
Cdd:COG1038 1115 TITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| COG3608 |
COG3608 |
Predicted deacylase [General function prediction only]; |
63-120 |
9.39e-03 |
|
Predicted deacylase [General function prediction only];
Pssm-ID: 442826 [Multi-domain] Cd Length: 296 Bit Score: 37.90 E-value: 9.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446601663 63 QAVTAVEQAVPRYLTGLG-------------TIIAANTVTVRSRVDGqLIALHFQEGQQVKAGDLLAEI-DP 120
Cdd:COG3608 191 ESIEAGVRGILNVLRHLGmldgeapppplapPVLARGSEWVRAPAGG-LFEPLVELGDRVKKGDVLGRItDP 261
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