|
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: 780.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 1 MKGSNKSRWVIAIVIVVATVAAIWFWQSRSASQETAPGATKPAQHTPGSARRGLRSGPLAPVQAATATEEAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 161 SRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 241 PENDIATVLQAQKSGNQLKVEAWDRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTQQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 321 AVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEGAKVEVVEAHDASVSD 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 489126989 401 EKTAPRGYGKKGANS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-393 |
1.23e-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: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 66 TATEEAVPRYLTGLGTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 146 RDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 226 VVITQTHPIDLIFTLPENDIATVLQAQksgnqlKVEAWDRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQ------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 306 NQFVNARMLVDTQQNAVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
....*...
gi 489126989 386 AKVEVVEA 393
Cdd:COG0845 314 AKVRVVEA 321
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
1.12e-77 |
|
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: 243.38 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 62 VQAATATEEAVPRYLTGLGTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 142 ANARRDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 222 TtgIVVITQTHPIDLIFTLPENDIATVlqaqKSGNQLKVEAwdRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 302 ALFPNQFVNARMLVDTQQNAVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 489126989 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 |
2.92e-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: 127.15 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 161 SRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 241 PENDIATVLQAQKSGNQLKVEAWDRTNSQKLSE-----------GVLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLQIAEAEAELKLAKLDlerteirapvdGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489126989 309 VNARMLVDTQQNAVVIPTAALQMGNEGHF-VWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVT 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 |
2.83e-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: 2.83e-04
10 20 30
....*....|....*....|....*....|
gi 489126989 89 TVRSRVDGQLIALHFEEGQQVKAGDLLAEI 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: 780.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 1 MKGSNKSRWVIAIVIVVATVAAIWFWQSRSASQETAPGATKPAQHTPGSARRGLRSGPLAPVQAATATEEAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 161 SRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 241 PENDIATVLQAQKSGNQLKVEAWDRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTQQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 321 AVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEGAKVEVVEAHDASVSD 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 489126989 401 EKTAPRGYGKKGANS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-393 |
1.23e-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: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 66 TATEEAVPRYLTGLGTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 146 RDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 226 VVITQTHPIDLIFTLPENDIATVLQAQksgnqlKVEAWDRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQ------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 306 NQFVNARMLVDTQQNAVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
....*...
gi 489126989 386 AKVEVVEA 393
Cdd:COG0845 314 AKVRVVEA 321
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
1.12e-77 |
|
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: 243.38 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 62 VQAATATEEAVPRYLTGLGTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 142 ANARRDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 222 TtgIVVITQTHPIDLIFTLPENDIATVlqaqKSGNQLKVEAwdRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 302 ALFPNQFVNARMLVDTQQNAVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 489126989 382 LTEGAKVEVV 391
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
80-392 |
1.39e-42 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 154.10 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 80 GTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNL 159
Cdd:PRK15030 58 GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 160 VSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFT 239
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 240 LPENDIATVLQAQKSGN------QLKVEAWDRTNSQKLSEGVLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARM 313
Cdd:PRK15030 218 QSSNDFLRLKQELANGTlkqengKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 314 LVDTQQNAVVIPTAALQMGNEGH-FVWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEGAKVEVVE 392
Cdd:PRK15030 298 EEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQE 377
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
48-397 |
9.05e-42 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 151.48 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 48 GSARRGLRSGPLAPVQAATATEEAVPRYLTGLGTITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVAL 127
Cdd:PRK09578 24 GKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 128 AQAQGQLAKDKATLANARRDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVG 207
Cdd:PRK09578 104 DAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 208 LKQVDVGNQISSGDTTGIVVITQTHPIDLIFTLPENDIATVLQAQKSGNQLKVEAWDRTNSQKLSEGV-------LLSLD 280
Cdd:PRK09578 184 RALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSeyplkgkLLFSD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 281 NQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTQQNAVVIPTAALQMGNEGHFVWVLNSDNKVSKHLVKPGIQDSQ 360
Cdd:PRK09578 264 LAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGR 343
|
330 340 350
....*....|....*....|....*....|....*..
gi 489126989 361 KVVIAAGLSAGDRVVTDGIDRLTEGAKVEVVEAHDAS 397
Cdd:PRK09578 344 DWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAA 380
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
88-401 |
6.88e-41 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 149.09 E-value: 6.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 88 ATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLVSRQELDA 167
Cdd:PRK09859 62 AEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 168 QQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFTLPENDIAT 247
Cdd:PRK09859 142 ARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 248 VLQAQKSGNQLKVE-----AWDRTNSQKLSE-GVLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTQQNA 321
Cdd:PRK09859 222 MKEEVASGQIKQVQgstpvQLNLENGKRYSQtGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 322 VVIPTAALQMGNEGHFV-WVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVTDGIDRLTEGAKVEVVEAHDASVSD 400
Cdd:PRK09859 302 LLVPQEGVTHNAQGKATaLILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENAST 381
|
.
gi 489126989 401 E 401
Cdd:PRK09859 382 E 382
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
81-376 |
2.92e-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: 127.15 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLVKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 161 SRQELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLIFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 241 PENDIATVLQAQKSGNQLKVEAWDRTNSQKLSE-----------GVLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLQIAEAEAELKLAKLDlerteirapvdGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489126989 309 VNARMLVDTQQNAVVIPTAALQMGNEGHF-VWVLNSDNKVSKHLVKPGIQDSQKVVIAAGLSAGDRVVT 376
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-316 |
8.41e-32 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 123.23 E-value: 8.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 1 MKGSNKSRWVIAIVIVVATVAAIWFWQSRSASQETapgatkpaqhtpgsarrglrsgplapvqaatateeavprylTGLG 80
Cdd:COG1566 1 MKALKKRRLLALVLLLLALGLALWAAGRNGPDEPV-----------------------------------------TADG 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAaNTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA------------------------- 135
Cdd:COG1566 40 RVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaq 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 136 --KDKATLANARRDLARYQQLVKTNLVSRQELDAQQALVNETLGTIKAD---------------------------EASV 186
Cdd:COG1566 119 laAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeeelaaaqaqvaqaEAAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 187 ASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLIFTLPENDIATVLQAQKSgnQLKVEAWDrt 266
Cdd:COG1566 199 AQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDLGRVKPGQPV--EVRVDAYP-- 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489126989 267 nSQKLsEGVLLSLDNQIDATTG----------TIKVKARFNNQD-DALFPNQFVNARMLVD 316
Cdd:COG1566 273 -DRVF-EGKVTSISPGAGFTSPpknatgnvvqRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
1-376 |
1.99e-25 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 106.40 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 1 MKGSNKSRWVIAIVIVVatVAAIWFWQSRSAsqetapgatkpaqhtpgsarrglrsgPLAPVQAATATEEAVPRYLTGLG 80
Cdd:PRK11578 3 KRKKVKKRYLIALVIVL--AGGITLWRILNA--------------------------PVPTYQTLIVRPGDLQQSVLATG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 81 TITAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFK-------VALAQAQGQLAKDKATLANARRDLARYQQ 153
Cdd:PRK11578 55 KLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLMELRAQRQQAEAELKLARVTLSRQQR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 154 LVKTNLVSRQELD-------AQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVglkqvdvgNQISS--GDTtg 224
Cdd:PRK11578 135 LAKTQAVSQQDLDtaatelaVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEV--------TQITTlqGQT-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 225 iVVITQTHPIdlIFTLPenDIATVL-QAQKSGN---QLK--VEAWDRT--NSQKLSEGVLLSLDNQIDATTGTIKVKARF 296
Cdd:PRK11578 205 -VIAAQQAPN--ILTLA--DMSTMLvKAQVSEAdviHLKpgQKAWFTVlgDPLTRYEGVLKDILPTPEKVNDAIFYYARF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 297 N--NQDDALFPNQFVNARMLVDTQQNAVVIPTAAL--QMGNEGHFVWVLNsDNKVSKHLVKPGIQDSQKVVIAAGLSAGD 372
Cdd:PRK11578 280 EvpNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALgdPVGDNRYKVKLLR-NGETREREVTIGARNDTDVEIVKGLEAGD 358
|
....
gi 489126989 373 RVVT 376
Cdd:PRK11578 359 EVII 362
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
85-244 |
4.59e-14 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 72.75 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 85 ANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARR------------------ 146
Cdd:PRK10476 46 ADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRsvdaersnaasaneqver 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 147 ----------DLARYQQLVKTNLVSRQELD---------------------AQQALVNET---LGTIKADEASVASAQLQ 192
Cdd:PRK10476 126 aranaklatrTLERLEPLLAKGYVSAQQVDqartaqrdaevslnqallqaqAAAAAVGGVdalVAQRAAREAALAIAELH 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489126989 193 LDWSRITAPVDGRVglkqvdVGNQISSGDTTGivvitqthPIDLIFTLPEND 244
Cdd:PRK10476 206 LEDTTVRAPFDGRV------VGLKVSVGEFAA--------PMQPIFTLIDTD 243
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
93-234 |
4.81e-14 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 72.69 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 93 RVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLA--------------------------NARR 146
Cdd:PRK03598 49 RVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkqaqaaydYAQN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 147 DLARYQQLVKTNLVSRQELD---------------AQQALVNETLGT-----------IKADEASVASAQLQLDWSRITA 200
Cdd:PRK03598 129 FYNRQQGLWKSRTISANDLEnarssrdqaqatlksAQDKLSQYREGNrpqdiaqakasLAQAQAALAQAELNLQDTELIA 208
|
170 180 190
....*....|....*....|....*....|....
gi 489126989 201 PVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPI 234
Cdd:PRK03598 209 PSDGTILTRAVEPGTMLNAGST--VFTLSLTRPV 240
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
86-135 |
9.92e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 56.68 E-value: 9.92e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489126989 86 NTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA 135
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
84-220 |
1.83e-10 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 62.02 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 84 AANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKD---------------------KATLA 142
Cdd:PRK15136 58 AGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyqanielqKTALA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 143 NARRDLARYQQLVKTNLVSRQEL---------------------DAQQALVnetLGT-------IKADEASVASAQLQLD 194
Cdd:PRK15136 138 QAQSDLNRRVPLGNANLIGREELqhardavasaqaqldvaiqqyNANQAMI---LNTpledqpaVQQAATEVRNAWLALQ 214
|
170 180
....*....|....*....|....*.
gi 489126989 195 WSRITAPVDGRVGLKQVDVGNQISSG 220
Cdd:PRK15136 215 RTKIVSPMTGYVSRRSVQVGAQISPT 240
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
84-222 |
1.77e-09 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 58.60 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 84 AANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLvKTNLVSRQ 163
Cdd:PRK10559 44 SADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSRE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489126989 164 ELDAQQALVNETLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDT 222
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGST 181
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
198-379 |
4.99e-07 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 51.41 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 198 ITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLIFTLPENdIATVLQAQkSGNQLKVEAWDRTnSQKLSEGVLL 277
Cdd:PRK09783 212 LKAPIDGVITAFDLRAGMNIAKDNV--VAKIQGMDPVWVTAAIPES-IAWLVKDA-SQFTLTVPARPDK-TFTIRKWTLL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 278 SldnQIDATTGTIKVKARFNNQDDALFPNqfVNARMLVDTQ-QNAVVIPTAAL-QMGNEGHFVWVLNSDNKVSKHLVKpg 355
Cdd:PRK09783 287 P---SVDAATRTLQLRLEVDNADEALKPG--MNAWLQLNTAsEPMLLIPSQALiDTGSEQRVITVDADGRFVPKRVAV-- 359
|
170 180
....*....|....*....|....*
gi 489126989 356 IQDSQKVV-IAAGLSAGDRVVTDGI 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 ... |
74-309 |
6.19e-07 |
|
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: 49.81 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 74 RYLTGLGTITA--ANTATVRSRVDGQLIALHF-EEGQQVKAGDLLAEIDPSQfkvaLAQAQGQLAkdkatLANARRDLAR 150
Cdd:pfam16576 4 RTIRAVGRVAYdeRRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPE----LVAAQQEYL-----LALRSGDALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 151 YQQLVKTnlvsrqeldAQQALVNetLGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTtgIVVITQ 230
Cdd:pfam16576 75 KSELLRA---------ARQRLRL--LGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDT--LFTIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 231 THPIDLIFTLPENDIATVlqaqKSGNQLKV-------EAWdrtnsqklsEGVLLSLDNQIDATTGTIKVKARFNNQDDAL 303
Cdd:pfam16576 142 LSTVWVEADVPEQDLALV----KVGQPAEVtlpalpgKTF---------EGKVDYIYPTLDPKTRTVRVRIELPNPDGRL 208
|
....*.
gi 489126989 304 FPNQFV 309
Cdd:pfam16576 209 KPGMFA 214
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
59-152 |
4.62e-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: 45.39 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126989 59 LAPV-QAATATEEAVPryltglgtitAANTATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDPSQFKVALAQAQGQlakd 137
Cdd:TIGR01843 24 FAPLdVVATATGKVVP----------SGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQ---- 89
|
90
....*....|....*
gi 489126989 138 katLANARRDLARYQ 152
Cdd:TIGR01843 90 ---VLRLEAEVARLR 101
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
89-118 |
2.83e-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: 2.83e-04
10 20 30
....*....|....*....|....*....|
gi 489126989 89 TVRSRVDGQLIALHFEEGQQVKAGDLLAEI 118
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
88-120 |
2.89e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.12 E-value: 2.89e-03
10 20 30
....*....|....*....|....*....|...
gi 489126989 88 ATVRSRVDGQLIALHFEEGQQVKAGDLLAEIDP 120
Cdd:PRK12999 1114 TTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
88-118 |
4.84e-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: 4.84e-03
10 20 30
....*....|....*....|....*....|.
gi 489126989 88 ATVRSRVDGQLIALHFEEGQQVKAGDLLAEI 118
Cdd:COG1038 1114 TTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
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|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
89-139 |
7.68e-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: 35.80 E-value: 7.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489126989 89 TVRSRVDGQLIALHFEEGQQVKAGDLLAEI-DPSQFKVALAQAQGQLAKDKA 139
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEAFVPAADLGSLKK 52
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