|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-369 |
0e+00 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 704.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 1 MLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAP 80
Cdd:PRK09859 17 MLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 81 LQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPI 160
Cdd:PRK09859 97 LQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 161 TGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTL 240
Cdd:PRK09859 177 TGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 241 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEAS 320
Cdd:PRK09859 257 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEAS 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 485707833 321 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ 369
Cdd:PRK09859 337 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ 385
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
24-361 |
2.52e-99 |
|
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: 297.24 E-value: 2.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 24 TLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNAR 103
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 104 ITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQAdsL 183
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 184 VTVQRLDPIYVDLTQSVQDFLRMKEevasGQikqvqgstPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNP 263
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKV----GQ--------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 264 NGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 343
Cdd:COG0845 228 DGLLRPGMFVRVRIVLGERENALLVPASAVVRD-GGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*...
gi 485707833 344 LQRIRPGIKARAISSSQE 361
Cdd:COG0845 307 LQRLRDGAKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
20-356 |
2.29e-80 |
|
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: 248.77 E-value: 2.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 20 VGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTA 99
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 100 SNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQ 179
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 180 AdsLVTVQRLDPIYVDLTQSVQDFLRmkeeVASGQIKQvqgstpVQLNLENGKRYSqtGTLKFSDPTVDETTGSVTLRAI 259
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQ----LRRGQTLT------VELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 260 FPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRV 339
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIED-LNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 485707833 340 IVSGLQRIRPGIKARAI 356
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
27-341 |
4.48e-80 |
|
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: 248.11 E-value: 4.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 27 PGSVNVLSELPGRTVPYEVAE-IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARIT 105
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 106 FNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVT 185
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 186 VQRLDPIYVDLTQSVQDFLR-MKEEVASGQIKQVQGSTPVQLNLENGKRYSQT----GTLKFSDPTVDETTGSVTLRAIF 260
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 261 PNP-NGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRV 339
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 485707833 340 IV 341
Cdd:pfam00529 321 RL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-369 |
0e+00 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 704.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 1 MLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAP 80
Cdd:PRK09859 17 MLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 81 LQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPI 160
Cdd:PRK09859 97 LQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 161 TGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTL 240
Cdd:PRK09859 177 TGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 241 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEAS 320
Cdd:PRK09859 257 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEAS 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 485707833 321 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ 369
Cdd:PRK09859 337 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ 385
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
2-369 |
2.84e-141 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 406.79 E-value: 2.84e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 2 LTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPL 81
Cdd:PRK15030 22 LTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 82 QAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPIT 161
Cdd:PRK15030 102 QATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPIS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 162 GVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLK 241
Cdd:PRK15030 182 GRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 242 FSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASK 321
Cdd:PRK15030 262 FSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQ 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 485707833 322 AIGDQWVVTSGLQAGDRVIVSGLQRIRPG--IKARAISSSQENASTESKQ 369
Cdd:PRK15030 342 AIGDKWLVTEGLKAGDRVVISGLQKVRPGvqVKAQEVTADNNQQAASGAQ 391
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
24-361 |
2.52e-99 |
|
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: 297.24 E-value: 2.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 24 TLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNAR 103
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 104 ITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQAdsL 183
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 184 VTVQRLDPIYVDLTQSVQDFLRMKEevasGQikqvqgstPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNP 263
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKV----GQ--------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 264 NGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 343
Cdd:COG0845 228 DGLLRPGMFVRVRIVLGERENALLVPASAVVRD-GGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*...
gi 485707833 344 LQRIRPGIKARAISSSQE 361
Cdd:COG0845 307 LQRLRDGAKVRVVEAAAP 324
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
2-356 |
1.81e-87 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 268.97 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 2 LTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPL 81
Cdd:PRK09578 20 LAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 82 QAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPIT 161
Cdd:PRK09578 100 KAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPID 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 162 GVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQV-QGSTPVQLNLENGKRYSQTGTL 240
Cdd:PRK09578 180 GRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGIaQQDVAVTLVRADGSEYPLKGKL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 241 KFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQgKATALILDKDDVVQLREIEAS 320
Cdd:PRK09578 260 LFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTAD-SASVKVVGQNGKVRDVEVEAD 338
|
330 340 350
....*....|....*....|....*....|....*.
gi 485707833 321 KAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAI 356
Cdd:PRK09578 339 QMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAV 374
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
20-356 |
2.29e-80 |
|
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: 248.77 E-value: 2.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 20 VGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTA 99
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 100 SNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQ 179
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 180 AdsLVTVQRLDPIYVDLTQSVQDFLRmkeeVASGQIKQvqgstpVQLNLENGKRYSqtGTLKFSDPTVDETTGSVTLRAI 259
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQ----LRRGQTLT------VELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 260 FPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRV 339
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIED-LNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305
|
330
....*....|....*..
gi 485707833 340 IVSGLQRIRPGIKARAI 356
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
27-341 |
4.48e-80 |
|
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: 248.11 E-value: 4.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 27 PGSVNVLSELPGRTVPYEVAE-IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARIT 105
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 106 FNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVT 185
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 186 VQRLDPIYVDLTQSVQDFLR-MKEEVASGQIKQVQGSTPVQLNLENGKRYSQT----GTLKFSDPTVDETTGSVTLRAIF 260
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 261 PNP-NGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRV 339
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320
|
..
gi 485707833 340 IV 341
Cdd:pfam00529 321 RL 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
48-369 |
3.14e-45 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 160.34 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 48 IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTAR 127
Cdd:PRK11556 90 VRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 128 TQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMK 207
Cdd:PRK11556 170 ALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDIATVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 208 EEVASGQikqvqgSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLL 287
Cdd:PRK11556 250 QAQKAGK------PLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 288 VPQEGVTHNAQGKATaLILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIK-----ARAISSSQEN 362
Cdd:PRK11556 324 IPTAALQMGNEGHFV-WVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKvevvePQSATTPEEK 402
|
....*..
gi 485707833 363 ASTESKQ 369
Cdd:PRK11556 403 ATSREYA 409
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
40-280 |
1.71e-26 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 107.83 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 40 TVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA-------------------------- 93
Cdd:COG1566 40 RVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaql 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 94 -KALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTV---------------------------AKAAVE 145
Cdd:COG1566 120 aAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAaqaqlaqaqaglreeeelaaaqaqvaqAEAALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 146 QATINLQYANVTSPITGVSGKSSVTVGALVTANQadSLVTVQRLDPIYVDLtqsvqdflrmkeEVASGQIKQVQGSTPVQ 225
Cdd:COG1566 200 QAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQ--PLLTIVPLDDLWVEA------------YVPETDLGRVKPGQPVE 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485707833 226 LNLENGKRYSQTGTLKF------SDPTVDETTGSVTLR-----AIFPNPNGDLLPGMYVTALVDEG 280
Cdd:COG1566 266 VRVDAYPDRVFEGKVTSispgagFTSPPKNATGNVVQRypvriRLDNPDPEPLRPGMSATVEIDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
51-350 |
5.41e-16 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 78.28 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 51 QVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQ-------AELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDY 123
Cdd:PRK11578 67 QVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 124 DTART-------QLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALV-TANQADSLVTVQRLDPIYVD 195
Cdd:PRK11578 147 DTAATelavkqaQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTViAAQQAPNILTLADMSTMLVK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 196 LTQSVQDFLRMKeevaSGQIK--QVQGstpvqlnlENGKRYSqtGTLKFSDPTVDETTGSVTLRAIF--PNPNGDLLPGM 271
Cdd:PRK11578 227 AQVSEADVIHLK----PGQKAwfTVLG--------DPLTRYE--GVLKDILPTPEKVNDAIFYYARFevPNPNGLLRLDM 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485707833 272 YVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSglqRIRPG 350
Cdd:PRK11578 293 TAQVHIQLTDVKNVLTIPLSALGDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIG---EAKPG 368
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
52-282 |
1.54e-13 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 70.76 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 52 VGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGS--------------------------LAKALSTASNARIT 105
Cdd:PRK03598 50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANvsvaqaqldlmlagyrdeeiaqaraaVKQAQAAYDYAQNF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 106 FNRQASLLKTNYVSRQDYDTARTQLN--------------------------EAEANVTVAKAAVEQATINLQYANVTSP 159
Cdd:PRK03598 130 YNRQQGLWKSRTISANDLENARSSRDqaqatlksaqdklsqyregnrpqdiaQAKASLAQAQAALAQAELNLQDTELIAP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 160 ITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIYVdltqsvqdflrmKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGT 239
Cdd:PRK03598 210 SDGTILTRAVEPGTMLNA--GSTVFTLSLTRPVWV------------RAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQ 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 485707833 240 LKFSDPTVDETTGSVT-----------LRAIFPNPNGDLLPGMYVTALVDEGSR 282
Cdd:PRK03598 276 IGFVSPTAEFTPKTVEtpdlrtdlvyrLRIVVTDADDALRQGMPVTVRFADEAG 329
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
45-273 |
4.95e-12 |
|
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: 64.45 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 45 VAEIRPQVGGIIIK--RNFiEGDKVNQGDSLYQIDpAPlqaELNSAKGSLAKALSTASNARitfnrqasllktnyvSRQD 122
Cdd:pfam16576 19 LAHVHARVEGWIEKlyVNA-TGDPVKKGQPLAELY-SP---ELVAAQQEYLLALRSGDALS---------------KSEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 123 YDTARTQL-----NEAEAnvtvakAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIYVDLt 197
Cdd:pfam16576 79 LRAARQRLrllgmPEAQI------AELERTGKVQPTVTVYAPISGVVTELNVREGMYVQP--GDTLFTIADLSTVWVEA- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485707833 198 qsvqdflrmkeEVASGQIKQVQGSTPVQLNLEN--GKRYsqTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYV 273
Cdd:pfam16576 150 -----------DVPEQDLALVKVGQPAEVTLPAlpGKTF--EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
44-180 |
6.28e-12 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 65.82 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 44 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA---KALST--------ASNARI-------- 104
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladAQIMTtqrsvdaeRSNAASaneqvera 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 105 ---------TFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVA------------------------KAAVEQATINL 151
Cdd:PRK10476 127 ranaklatrTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQAllqaqaaaaavggvdalvaqraarEAALAIAELHL 206
|
170 180
....*....|....*....|....*....
gi 485707833 152 QYANVTSPITGVSGKSSVTVGALVTANQA 180
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQP 235
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
46-195 |
7.32e-07 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 50.46 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 46 AEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAK------------------------ALSTASN 101
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANsvrqthqlminskqyqanielqktALAQAQS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 102 ariTFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKA------------------AVEQAT-------INLQYANV 156
Cdd:PRK15136 142 ---DLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQqynanqamilntpledqpAVQQAAtevrnawLALQRTKI 218
|
170 180 190
....*....|....*....|....*....|....*....
gi 485707833 157 TSPITGVSGKSSVTVGALVTANQadSLVTVQRLDPIYVD 195
Cdd:PRK15136 219 VSPMTGYVSRRSVQVGAQISPTT--PLMAVVPATNLWVD 255
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
44-93 |
3.86e-06 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 43.59 E-value: 3.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 485707833 44 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA 93
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
245-344 |
5.88e-06 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 47.94 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 245 PTVDETTGSVTLRAIFPNPNGDLLPGMYVT----------------ALVDEGSRQNVLLVPQEG--------VTHNAQGK 300
Cdd:PRK09783 287 PSVDAATRTLQLRLEVDNADEALKPGMNAWlqlntasepmllipsqALIDTGSEQRVITVDADGrfvpkrvaVFQESQGV 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 485707833 301 AtalildkddvvqlreieaskAIGdqwvvtSGLQAGDRVIVSGL 344
Cdd:PRK09783 367 T--------------------AIR------SGLAEGEKVVSSGL 384
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
156-270 |
2.56e-05 |
|
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: 42.73 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 156 VTSPITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVasgqikqvqgstPVQLNLENGKRYS 235
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQA--GDPLATIVPPDRLLVEAFVPAADLGSLKKGQ------------KVTLKLDPGSDYT 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 485707833 236 QTGTLKFSDPTVDETTGSVTLRAIFPNPNGD--LLPG 270
Cdd:pfam13437 68 LEGKVVRISPTVDPDTGVIPVRVSIENPKTPipLLPG 104
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
44-162 |
1.40e-03 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 40.11 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485707833 44 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASlLKTNYVSRQDY 123
Cdd:PRK10559 46 DVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNR-LGVQAMSREEI 124
|
90 100 110
....*....|....*....|....*....|....*....
gi 485707833 124 DTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITG 162
Cdd:PRK10559 125 DQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADG 163
|
|
| |
