ID   FARB_NEIGO              Reviewed;         507 AA.
AC   Q9RQ29;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Fatty acid resistance protein FarB {ECO:0000305};
DE   AltName: Full=Efflux pump protein FarB {ECO:0000305};
GN   Name=farB {ECO:0000303|PubMed:10447892};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=FA19;
RX   PubMed=10447892; DOI=10.1046/j.1365-2958.1999.01530.x;
RA   Lee E.H., Shafer W.M.;
RT   "The farAB-encoded efflux pump mediates resistance of gonococci to long-
RT   chained antibacterial fatty acids.";
RL   Mol. Microbiol. 33:839-845(1999).
RN   [2]
RP   INDUCTION.
RC   STRAIN=FA19;
RX   PubMed=14645274; DOI=10.1128/jb.185.24.7145-7152.2003;
RA   Lee E.H., Rouquette-Loughlin C., Folster J.P., Shafer W.M.;
RT   "FarR regulates the farAB-encoded efflux pump of Neisseria gonorrhoeae via
RT   an MtrR regulatory mechanism.";
RL   J. Bacteriol. 185:7145-7152(2003).
CC   -!- FUNCTION: Mediates resistance to long-chained antibacterial fatty acids
CC       (FAs) (PubMed:10447892). Function is dependent on the MtrE outer
CC       membrane protein (PubMed:10447892). {ECO:0000269|PubMed:10447892}.
CC   -!- SUBUNIT: Probably part of a tripartite efflux system FarAB-MtrE, which
CC       is composed of an inner membrane transporter, FarB, a periplasmic
CC       membrane fusion protein, FarA, and an outer membrane component, MtrE.
CC       {ECO:0000305|PubMed:10447892}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by MtrR (PubMed:10447892,
CC       PubMed:14645274). MtrR acts by modulating the expression of the
CC       regulatory protein FarR, which directly controls the expression of the
CC       farAB operon (PubMed:14645274). {ECO:0000269|PubMed:10447892,
CC       ECO:0000269|PubMed:14645274}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is hypersusceptible to long-chained fatty
CC       acids such as palmitic acid, oleic acid and linoleic acid.
CC       {ECO:0000269|PubMed:10447892}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC       {ECO:0000305}.
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DR   EMBL; AF132910; AAD54074.1; -; Genomic_DNA.
DR   RefSeq; WP_017146881.1; NZ_CP012026.1.
DR   AlphaFoldDB; Q9RQ29; -.
DR   SMR; Q9RQ29; -.
DR   TCDB; 2.A.1.3.20; the major facilitator superfamily (mfs).
DR   PATRIC; fig|485.48.peg.1747; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR004638; EmrB-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..507
FT                   /note="Fatty acid resistance protein FarB"
FT                   /id="PRO_0000445984"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   507 AA;  54798 MW;  CE4103DD11A1F4A4 CRC64;
     MDYPPLKGAA LAWVTLSLGL AVFMEVLDTT IANVAVPVIA GNLGAATTQG TWVITSFSVA
     NAVSVPLTGF LAKRIGEVKL FTAAAAGFVI ASWLCGIAPN LQSLVVFRIL QGFIAGPLIP
     LSQSLLMASY PPAKRMLALA LWAMTVVVAP VLGPILGGWI SGNWHWGWIF FINIPIGIIS
     AWITWKHLKH RETATVRTPT DYVGLTLMMV GIGALQMMLD RGKELDWFAS GEIITLGITA
     LVCLSYFIVW ELGEKYPIVD LSLFKDRNFT VGAIATSLGF MVYMGTLTLL PLVLQTNLGY
     TSAWAGLAAA PVGILPVFLS PLIGRFGNKI DMRLLVTASF LTFAFTFYWR TDFYADMDIG
     NVIWPQFWQG VGVAMFFLPL TTITLSHMKG GQIAAAGSLS NFLRVLMGGV GVSVVSTLWE
     RREALHHTRF AEHITPYSAT LHETAAHLSQ QGISDGQTLG IINNTITQQG FIIGSNEIFL
     AGSILFIVLI PIVWLAKPPF HSGGGGH