ID A0A1I5TNA8_9SPHN Unreviewed; 1081 AA.
AC A0A1I5TNA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Efflux pump membrane transporter {ECO:0000256|RuleBase:RU364070};
GN ORFNames=SAMN04488241_108123 {ECO:0000313|EMBL:SFP83816.1};
OS Sphingomonas rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP83816.1, ECO:0000313|Proteomes:UP000199586};
RN [1] {ECO:0000313|EMBL:SFP83816.1, ECO:0000313|Proteomes:UP000199586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP83816.1,
RC ECO:0000313|Proteomes:UP000199586};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|RuleBase:RU364070}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|RuleBase:RU364070}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000256|ARBA:ARBA00010942,
CC ECO:0000256|RuleBase:RU364070}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU364070}.
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DR EMBL; FOXP01000008; SFP83816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5TNA8; -.
DR STRING; 634430.SAMN04488241_108123; -.
DR OrthoDB; 9807350at2; -.
DR Proteomes; UP000199586; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042908; P:xenobiotic transport; IEA:InterPro.
DR Gene3D; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2.
DR Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 1.
DR Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004764; MdtF-like.
DR NCBIfam; TIGR00915; 2A0602; 1.
DR PANTHER; PTHR32063; -; 1.
DR PANTHER; PTHR32063:SF13; MULTIDRUG EFFLUX PUMP SUBUNIT ACRB-RELATED; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU364070};
KW Cell membrane {ECO:0000256|RuleBase:RU364070};
KW Membrane {ECO:0000256|RuleBase:RU364070};
KW Reference proteome {ECO:0000313|Proteomes:UP000199586};
KW Transmembrane {ECO:0000256|RuleBase:RU364070};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364070};
KW Transport {ECO:0000256|RuleBase:RU364070}.
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 366..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 470..497
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 549..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 881..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 905..925
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 931..954
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 975..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT TRANSMEM 1008..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364070"
FT REGION 1044..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 114815 MW; AECB21CE8CBBCF21 CRC64;
MSRYFIDRPI FAFVIAIVLM LAGALAIRTL PIAQFPTIAP PAVAINVVYP GADAETIERT
TTQIIEQQLK GIDNLRYFSS SSTSAGAATI TLTFEQGADP DIAQVQVQNK VAAATPLLPQ
EVQRQGVQVQ KSANNFLLVV GLYSENGDHD GADLADYVVS RLQDPISRVN GVGEAQVFGS
QYAMRIWVDP IKLASYQLTM ADVTAAVTAQ NAQVSAGQIG GLPAPKEQML NATVSVQSRL
QTPQEFANIR LKTAASGAVV RLSDVARVAL GSENYGFDLK YNGHPASGFG IRLAPGANAL
DTVTAVKDEV ARIAKGFPPD VKVVYPYDTT PFVRLSVEQV VHTLIEAVVL VFLVMFLFLQ
NWRATIIPTI AVPVVLLGTF AVMALAGYSI NTLTLFGMVL AIGLLVDDAI VVVENVERLI
QTEGLSPKEA ARKSMDEITG ALVGIALVLS AVFLPMAFFG GSTGVIYRQF SITIVSAMVL
SIMVALILTP ALCATILKPH DPARHHEPKP GIRGWPQRFF NWFNDKFDRG QVKYERGVKR
TARSWKRSFL VYFLIVLGMG FLFVRMPTGF LPDEDQGYLI ALVQGPSGAT AGRTDKALDT
VRDHFLKSES ANVKGVFTIS GFSFAGQGQN AGLAFINLKD WEERSGAENK AAAIAGRAMG
PLSQFHDAMI FALSPPAVSE LGNATGFDLW LTDTGGAGHA GLLAKRNQML GMAMGDKGVT
QVRPLSLDDA AQLNVEVDQD KARALGLDLS EINSTISTAW GGAYVNDFID RGRVKRVYLQ
ADTPYRLNPA SIGDFFVRGA SGQMAPFTAF STQSWTKAPV QLTRYNGVPA FEIQGAPAPG
LSTGSAMDAM EAIHDKLPPG TGLSWTGLSY EEQLSGGQAP ALYALSLIIV FLCLAALYES
WSVPIAVMLV VPLGVVGALL AASLTGLNND IYLQVGLITT IGVAAKNAIL IVEFAEERLR
DGMSPFDAAV EAAKLRLRPI LMTSLAFVFG VLPLALSTGA GAGGQNAIGR AVVGGMLSAT
VLAIFFVPMF FVTVSRLFGH GKEDAGGAGS SANADKPNAS SDITPDGGNR SSDGGEAPQG
A
//
