|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
6-349 |
0e+00 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 507.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 6 GSERKRRLALIVAGVIVVAAVISGWlsvrQTTLNPLSEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPD 85
Cdd:PRK10476 7 KSPRKKLPALAIVALAIVALVFVIW----RTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 86 LYRLQVEQAQAELKMAEAARDTQQRTVVAEQSNAAITNEQIVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAATAKH 165
Cdd:PRK10476 83 PYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 166 DAEVSLKQALKQSFAAEALVSSTAASEALVVARRAALAIAERELANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINT 245
Cdd:PRK10476 163 DAEVSLNQALLQAQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 246 EHWHASAFFRETELKHIKVGDCATVYVMADRQRAIQGRVEGIGWGVSSEDMLNIPRGLPYVPKSLNWVRVVQRFPVRISL 325
Cdd:PRK10476 243 DHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIML 322
|
330 340
....*....|....*....|....
gi 517908828 326 EKPPEDLMRIGATAVVIVRNDEGC 349
Cdd:PRK10476 323 DKPDPELFRIGASAVVELRPGAAC 346
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
30-344 |
3.01e-68 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 217.22 E-value: 3.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 30 WLSVRQTTLNPLSEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAARDTQQ 109
Cdd:COG1566 24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 110 RTVVAEQSNAAItNEQIVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALKQSFAAEALVSST- 188
Cdd:COG1566 104 AELGAEAEIAAA-EAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEe 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 189 --AASEALVVARRAALAIAERELANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGD 266
Cdd:COG1566 183 elAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQ 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517908828 267 CATVYVMADRQRAIQGRVEGIGWGVSSEDMLNIPRGlpyvpkslnwvRVVQRFPVRISLEKPPEDLMRIGATAVVIVR 344
Cdd:COG1566 263 PVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATG-----------NVVQRYPVRIRLDNPDPEPLRPGMSATVEID 329
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
40-341 |
1.64e-58 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 192.32 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 40 PLSEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAelKMAEAARDTQQ--RTVVAEQS 117
Cdd:TIGR00998 31 ESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAELALAKAEA--NLAALVRQTKQleITVQQLQA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 118 NAAITNEQIVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALKQSFAA-EALVSSTAASEAL-V 195
Cdd:TIGR00998 109 KVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKALLSAKAALNAAIQEQLNAnQALVRGTPLKKQPaV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 196 VARRAALAIAERELANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVYV-MA 274
Cdd:TIGR00998 189 QEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSdLY 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517908828 275 DRQRAIQGRVEGIGWGVSsedmlNIPRGLPYVPKSLNWVRVVQRFPVRISLEKPPED--LMRIGATAVV 341
Cdd:TIGR00998 269 GSDVVFEGKVTGISMGTG-----SAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDehPLRIGLSAEV 332
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
52-347 |
2.01e-38 |
|
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: 139.31 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 52 VHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKmaeaardtqqrtvvaeqsnaaitneqivRAQA 131
Cdd:COG0845 24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLA----------------------------AAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 132 NLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQAlkqsfaaealvsstaasealvvarRAALAIAERELAN 211
Cdd:COG0845 76 QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAA------------------------QAALEQARANLAY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 212 TQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVYVMADRQRAIQGRVEGIGWGV 291
Cdd:COG0845 132 TTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAV 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 517908828 292 SSEdmlniprglpyvpkslnwvrvVQRFPVRISLEKPPEDLmRIGATAVVIVRNDE 347
Cdd:COG0845 212 DPA---------------------TRTVRVRAELPNPDGLL-RPGMFVRVRIVLGE 245
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-307 |
1.14e-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: 126.77 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 40 PLSEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAARDTQQRTV------- 112
Cdd:pfam00529 9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELdrlqale 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 113 ----VAEQSNAAIT------NEQIVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALKQSFAAE 182
Cdd:pfam00529 89 selaISRQDYDGATaqlraaQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 183 ALVSSTAA------------SEALVVARRAALAIAERELANTQIRAPHDGRVVGLTVS-AGEFVVPDQAIFTLINTEHWH 249
Cdd:pfam00529 169 VQITQSAAenqaevrselsgAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLL 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517908828 250 ASAFFRETELKHIKVGDCATVYVMA---DRQRAIQGRVEGIGWGVSSEDMLNIPRGLPYVP 307
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAfpqTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYP 309
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
37-343 |
6.75e-28 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 110.60 E-value: 6.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 37 TLNPLSEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELK-----MAEAARDTQQRT 111
Cdd:PRK10559 33 TESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAyyqvlAQEKRREAGRRN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 112 VVAEQsnaAITNEQIVRAQANLKLATQTLARLQpllpkgyvtaqqvddaatakhdaevslkqalkqsfaaealvsstaas 191
Cdd:PRK10559 113 RLGVQ---AMSREEIDQANNVLQTVLHQLAKAQ----------------------------------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 192 ealvvarrAALAIAERELANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVY 271
Cdd:PRK10559 143 --------ATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEIT 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517908828 272 VMADrQRAIQGRVEGIGWGVSSEDMLNIPRGLPYVPKSLNWVRVVQRFPVRISLEKPPEDLMRIGATAVVIV 343
Cdd:PRK10559 215 PLGS-NKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTTATVVI 285
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
52-287 |
1.27e-26 |
|
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: 107.40 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 52 VHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAardtqqrtvvaeqsnaaitneqivraqa 131
Cdd:TIGR01730 27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEA---------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 132 NLKLATQTLARLQPLLPKGYVTAQQVDDAatakhdaevslKQALKqsfaaealvsstaASEALVVARRAALAIAERELAN 211
Cdd:TIGR01730 79 QLELAQRSFERAERLVKRNAVSQADLDDA-----------KAAVE-------------AAQADLEAAKASLASAQLNLRY 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517908828 212 TQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVYVMADRQRAIQGRVEGI 287
Cdd:TIGR01730 135 TEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFI 210
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
42-348 |
3.36e-24 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 102.08 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 42 SEDAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELkmAEAARDTQQRTVVAEQSNAAI 121
Cdd:PRK15136 52 TDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTAL--ANSVRQTHQLMINSKQYQANI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 122 TNEQIV--RAQANLKlatqtlaRLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALKQSFAAEALVSST------AASEA 193
Cdd:PRK15136 130 ELQKTAlaQAQSDLN-------RRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMILNTpledqpAVQQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 194 LVVARRAALAiaereLANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVyvM 273
Cdd:PRK15136 203 ATEVRNAWLA-----LQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATI--T 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 274 AD---RQRAIQGRVEGIGWGVSSEDMLniprgLPYVPKSLNWVRVVQRFPVRISLEkpPEDL----MRIGATAVVIV--R 344
Cdd:PRK15136 276 SDiygDDVVYTGKVVGLDMGTGSAFSL-----LPAQNATGNWIKVVQRLPVRIELD--AKQLaqhpLRIGLSTLVTVdtA 348
|
....
gi 517908828 345 NDEG 348
Cdd:PRK15136 349 NRDG 352
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
52-271 |
5.83e-18 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 83.47 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 52 VHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAARDTQQRTVVAEQsnAAITNEQIVRAQA 131
Cdd:PRK03598 44 VNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLAGYRDEE--IAQARAAVKQAQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 132 NLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSL---KQALKQsFAAEALVSSTAASEALVVARRAALAIAERE 208
Cdd:PRK03598 122 AYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLksaQDKLSQ-YREGNRPQDIAQAKASLAQAQAALAQAELN 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517908828 209 LANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVY 271
Cdd:PRK03598 201 LQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLY 263
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
52-287 |
1.13e-13 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 71.34 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 52 VHIASSVPGRIISINVEENSKVRRGDLLFSIEPdlyrlqvEQAQAELKMAEAARDTqqrtvvaeqsnaaiTNEQIVRAQA 131
Cdd:PRK11578 62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDP-------EQAENQIKEVEATLME--------------LRAQRQQAEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 132 NLKLATQTLARLQPLLPKGYVTAQQVDDAATakhdaEVSLKQAlkqsfaaealvsSTAASEALVVARRAALAIAERELAN 211
Cdd:PRK11578 121 ELKLARVTLSRQQRLAKTQAVSQQDLDTAAT-----ELAVKQA------------QIGTIDAQIKRNQASLDTAKTNLDY 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517908828 212 TQIRAPHDGRVVGLTVSAGEFVVPDQA---IFTLINTEHWHASAFFRETELKHIKVGDCATVYVMADRQRAIQGRVEGI 287
Cdd:PRK11578 184 TRIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDI 262
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
49-242 |
1.18e-11 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 65.20 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 49 ASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELkmaeaARDtqqrtvvaeqsnaaitneqivr 128
Cdd:PRK11556 85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQL-----AKD---------------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 129 aQANLKLATQTLARLQPLLPKGYVTAQQVDdaatakhdaevslkqalkqsfAAEALVSSTaasEALVVARRAALAIAERE 208
Cdd:PRK11556 138 -QATLANARRDLARYQQLAKTNLVSRQELD---------------------AQQALVSET---EGTIKADEASVASAQLQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517908828 209 LANTQIRAPHDGRV------VGLTVSAGE---FVV-----PDQAIFTL 242
Cdd:PRK11556 193 LDYSRITAPISGRVglkqvdVGNQISSGDttgIVVitqthPIDLVFTL 240
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
61-298 |
3.33e-11 |
|
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.
Pssm-ID: 213754 [Multi-domain] Cd Length: 327 Bit Score: 63.31 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 61 RIISINVEENSKVRRGDLLFSIEP-DLYRLQVEQAQAELKMAEA------------ARDTQQRTVVAEQSNAAITNEQ-- 125
Cdd:TIGR02971 26 RIKKLLVAEGDRVQAGQVLAELDSrPERTAELDVARTQLDEAKArlaqvragakkgEIAAQRAARAAAKLFKDVAAQQat 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 126 IVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALK----QSFAAEALVSSTAAS---------E 192
Cdd:TIGR02971 106 LNRLEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEALAsrseQIDGARAALASLAEEvretdvdlaQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 193 ALVVARRAALAIAERELANTQIRAPHDGRVVGLTVSAGEfVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVYV 272
Cdd:TIGR02971 186 AEVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGE-VIGSEGILEMGDTSQMYAVAEVYETDINRVRVGQRATITS 264
|
250 260
....*....|....*....|....*.
gi 517908828 273 MADRQRAiQGRVEGIGWGVSSEDMLN 298
Cdd:TIGR02971 265 TALSGPL-RGTVRRIGSLIAKNDVLS 289
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
51-99 |
8.17e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 56.68 E-value: 8.17e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 517908828 51 VVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELK 99
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| NHLM_micro_HlyD |
TIGR03794 |
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the ... |
51-288 |
7.26e-10 |
|
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the HlyD membrane fusion protein of type I secretion systems. Their occurrence in prokaryotic genomes is associated with the occurrence of a novel class of microcin (small bacteriocins) with a leader peptide region related to nitrile hydratase. We designate the class of bacteriocin as Nitrile Hydratase Leader Microcin, or NHLM. This family, therefore, is designated as NHLM bacteriocin system secretion protein. Some but not all NHLM-class putative microcins belong to the TOMM (thiazole/oxazole modified microcin) class as assessed by the presence of the scaffolding protein and/or cyclodehydratase in the same gene clusters. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274787 [Multi-domain] Cd Length: 421 Bit Score: 59.86 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 51 VVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEA---------ARDTQQRTVVAEQSNAAI 121
Cdd:TIGR03794 58 VDTIQSPGSGVVIDLDVEVGDQVKKGQVVARLFQPELRERLQESYQKLTQLQEqleevrnytGRLKEGRERHFQKSKEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 122 tNEQIVRAQANLKLATQTLARLQPLLPKGY-------VTAQQVD---------DAATA--------KHDAEVSLKQALKQ 177
Cdd:TIGR03794 138 -EETIGRLREELAALSREVGKQRGLLSRGLatfkrdrILQQQWReeqakydaaDKARAiyalqtkaDERNLETVLQSLSQ 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 178 SFAAEALVSS----TAASEALVVARRAALAIAERELaNTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTL----INTEHWH 249
Cdd:TIGR03794 217 ADFQLAGVAQqeleTVEARIKEARYEIEELENKLNL-NTRIVSQHSGRVIELNYTPGQLVAAGAPLASLevedQTDEGLE 295
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 517908828 250 ASAFFRETELKHIKVGDCATVY---VMADRQRAIQGRVEGIG 288
Cdd:TIGR03794 296 GVAYFPVAEGKKIRPGMSVQITpstVKAERDGYIRGTVTSVS 337
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
214-288 |
5.71e-09 |
|
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: 53.13 E-value: 5.71e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517908828 214 IRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEHWHASAFFRETELKHIKVGDCATVYVMADRQRAIQGRVEGIG 288
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRIS 76
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
51-238 |
2.28e-06 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 48.94 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 51 VVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELkmaeaardtqqrtvvaeqsnaaitneqiVRAQ 130
Cdd:PRK15030 65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDL----------------------------AKAQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 131 ANLKLATQTLARLQPLLPKGYVTAQQVDDAatakhdaevslkqalkqsfaaealVSSTAASEALVVARRAALAIAERELA 210
Cdd:PRK15030 117 AAANIAQLTVNRYQKLLGTQYISKQEYDQA------------------------LADAQQANAAVTAAKAAVETARINLA 172
|
170 180
....*....|....*....|....*...
gi 517908828 211 NTQIRAPHDGRVVGLTVSAGEFVVPDQA 238
Cdd:PRK15030 173 YTKVTSPISGRIGKSNVTEGALVQNGQA 200
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
68-230 |
9.60e-05 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.87 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 68 EENSKVRRGDLLFSIEPDL---YRLQVEQAQAELKMAEAARDTQQRTVVAEQSNAAIT----NEQIVRAQANLKLATQTL 140
Cdd:COG1538 27 RAQLRQARAGLLPSQELDLggkRRARIEAAKAQAEAAEADLRAARLDLAAEVAQAYFDllaaQEQLALAEENLALAEELL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 141 ARLQPLLPKGYVTAQQVDDAATAKHDAEVSLKQALKQSFAAEA-------------------------LVSSTAASEALV 195
Cdd:COG1538 107 ELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNalalllglpppapldlpdplpplppLPPSLPGLPSEA 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 517908828 196 VARRAALAIAEREL--ANTQIRAPHDGRVVGLTVSAG 230
Cdd:COG1538 187 LERRPDLRAAEAQLeaAEAEIGVARAAFLPSLSLSAS 223
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
53-83 |
1.06e-04 |
|
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: 44.30 E-value: 1.06e-04
10 20 30
....*....|....*....|....*....|.
gi 517908828 53 HIASSVPGRIISINVEENSKVRRGDLLFSIE 83
Cdd:COG1038 1078 HIGAPMPGTVVKVLVKEGDEVKKGDPLLTIE 1108
|
|
| outer_NodT |
TIGR01845 |
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ... |
76-203 |
1.76e-04 |
|
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]
Pssm-ID: 273830 [Multi-domain] Cd Length: 460 Bit Score: 43.17 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 76 GDLLFSIEPDL---YRLQVEQAQAELKMAEAARDTQQRTVVAEQSNAAItneQIVRAQANLKLATQTLARLQPLLPkgyV 152
Cdd:TIGR01845 128 LTLDVSYELDLfgkVRRAVESALAQLEAAEADSQAARLTLSASIANAYV---QLAALRAQLDVYHAALASRRKTLE---L 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 517908828 153 TAQQVDdaatAKHDAEVSLKQALKQSFAAEALVSSTAASEALVVARRAALA 203
Cdd:TIGR01845 202 TQKRYA----AGVAAASDVRQAEAAVASAEAELPSLDVQIAQARNALAALL 248
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
53-83 |
2.26e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 43.20 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|.
gi 517908828 53 HIASSVPGRIISINVEENSKVRRGDLLFSIE 83
Cdd:PRK12999 1078 HVGAPMPGSVVTVLVKEGDEVKAGDPLAVIE 1108
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
51-284 |
5.48e-04 |
|
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: 40.57 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 51 VVHIASSVPGRIISINV-EENSKVRRGDLLFSIE-PDLYrlqveQAQAELkmaeaardtqqrtVVAEQSNAAITNEQIVR 128
Cdd:pfam16576 19 LAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYsPELV-----AAQQEY-------------LLALRSGDALSKSELLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 129 AqanlklATQTLARLQpllpkgyVTAQQVddaatakhdaevslkqalkqsfaaealvsstaasealvvarrAALAIAERE 208
Cdd:pfam16576 81 A------ARQRLRLLG-------MPEAQI------------------------------------------AELERTGKV 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517908828 209 LANTQIRAPHDGRVVGLTVSAGEFVVPDQAIFTLINTEH-W-HASAFfrETELKHIKVGDCATVYVMADRQRAIQGRV 284
Cdd:pfam16576 106 QPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTvWvEADVP--EQDLALVKVGQPAEVTLPALPGKTFEGKV 181
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
87-183 |
7.76e-04 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 87 YRLQVEQAQAELKMAEAARDTQQRTVVAEQSNA----AITNEQIVRAQANLKLATQTLARLQPLLPKGYVTAQQVDDAAT 162
Cdd:pfam02321 74 RRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAylqlLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEV 153
|
90 100
....*....|....*....|.
gi 517908828 163 AKHDAEVSLKQALKQSFAAEA 183
Cdd:pfam02321 154 ELLEARLELLNAEADLELALA 174
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
29-178 |
1.74e-03 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 40.08 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 29 GWLSVRQTTLNPLSE--DAELGASVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAArd 106
Cdd:PRK09859 37 GVVTLSPGSVNVLSElpGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALST-- 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517908828 107 tqqrtvvaeQSNAAItneqivraqanlklatqTLARLQPLLPKGYVTAQQVDDAATAKHDAEVSL---KQALKQS 178
Cdd:PRK09859 115 ---------ASNARI-----------------TFNRQASLLKTNYVSRQDYDTARTQLNEAEANVtvaKAAVEQA 163
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
50-203 |
5.35e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 38.65 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 50 SVVHIASSVPGRIISINVEENSKVRRGDLLFSIEPDLYRLQVEQAQAELKMAEAARDTQQRTVVAEQSNAAITNEQIVrA 129
Cdd:PRK11855 160 ATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAA-A 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517908828 130 QANLKLATQT-----------LARLQPLLPKGYVTAQQVDDAAtakhdaevslKQALK-QSFAAEALVSSTAASEALVVA 197
Cdd:PRK11855 239 PGKAPHASPAvrrlarelgvdLSQVKGTGKKGRITKEDVQAFV----------KGAMSaAAAAAAAAAAAGGGGLGLLPW 308
|
....*.
gi 517908828 198 RRAALA 203
Cdd:PRK11855 309 PKVDFS 314
|
|
| |
