ID   FARA_NEIGO              Reviewed;         394 AA.
AC   Q9RQ30;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Fatty acid resistance protein FarA {ECO:0000305};
DE   AltName: Full=Efflux pump protein FarA {ECO:0000305};
GN   Name=farA {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, AND INDUCTION.
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}; Single-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   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; AF132909; AAD54073.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RQ30; -.
DR   SMR; Q9RQ30; -.
DR   TCDB; 8.A.1.1.2; the membrane fusion protein (mfp) family.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..394
FT                   /note="Fatty acid resistance protein FarA"
FT                   /id="PRO_0000445983"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  42528 MW;  14F4B953D2F64936 CRC64;
     MKSGNSEPNL METHTDETKL QNTQVKRKRR LTALTLLFAL SAAAAGSAFF LWWQHEEETE
     DAYVAGRVVQ VTPQKGGTVR KVLHDDTDAV KKGDVLAVLD DDNDVLAYER AKNELVQAVR
     QNRRQNAATS QAGAQVALRR ADLARAQDDL RRRSALAESG AVSAEELAHA RTAVSQAQAA
     VKAALAEESS ARAALGGDVS LREQPEVQTA IGRLKDAWLN LRRTQVRAPA DGQVAKRSVQ
     VGQQVAAGAP LMAVVPLSDV WVDANFKETQ LRHMKIGQPA ELVSDLYGKQ IVYRGRVAGF
     SAGTGSAFSL IPAQNATGNW IKVVQRVPVR IVLNREDVDR HPLRIGLSMT VKVDTSAAGA
     PVSKTPGAAL PEMESTDWSE VDRTVDEILG QSAP