ID   MEPA_PSEPU              Reviewed;         384 AA.
AC   P0C069;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Multidrug/solvent efflux pump periplasmic linker protein MepA;
DE   Flags: Precursor;
GN   Name=mepA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=KT2442-TOL;
RX   PubMed=9827328; DOI=10.1007/s007920050084;
RA   Fukumori F., Hirayama H., Takami H., Inoue A., Horikoshi K.;
RT   "Isolation and transposon mutagenesis of a Pseudomonas putida KT2442
RT   toluene-resistant variant: involvement of an efflux system in solvent
RT   resistance.";
RL   Extremophiles 2:395-400(1998).
CC   -!- FUNCTION: The periplasmic linker protein component of an organic
CC       solvent and antibiotic efflux pump; confers resistance to toluene,
CC       hexane, p-xylene, ampicillin, penicillin G, erythromycin, novobiocin
CC       and tetracycline.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: There are 4 nearly identical operons in various strains of
CC       P.putida. This one and the ttgABC operon of strain DOT-T1E function in
CC       solvent and antibiotic efflux; however in strain S12 the arpABC operon
CC       functions only in antibiotic efflux. This may be due to different
CC       protein expression levels. In strain KT2440 the equivalent operon does
CC       not seem to function in toluene efflux. {ECO:0000305}.
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DR   RefSeq; WP_010952494.1; NZ_LT799039.1.
DR   AlphaFoldDB; P0C069; -.
DR   SMR; P0C069; -.
DR   STRING; 1240350.AMZE01000001_gene2851; -.
DR   PATRIC; fig|303.175.peg.5271; -.
DR   eggNOG; COG0845; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR01730; RND_mfp; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Coiled coil;
KW   Lipoprotein; Membrane; Palmitate; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..384
FT                   /note="Multidrug/solvent efflux pump periplasmic linker
FT                   protein MepA"
FT                   /id="PRO_0000018711"
FT   REGION          362..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          115..155
FT                   /evidence="ECO:0000255"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   384 AA;  41250 MW;  16BB3FA87E3C16CA CRC64;
     MQFKPAVTAL VSAVALATLL SGCKKEEAAP AAQAPQVGVV TIQPQAFTLT SELPGRTSAY
     RVAEVRPQVN GIILKRLFKE GSEVKEGQQL YQIDPAVYEA TLANAKANLL ATRSLAERYK
     QLIDEQAVSK QEYDDANAKR LQAEASLKSA QIDLRYTKVL APISGRIGRS SFTEGALVSN
     GQTDAMATIQ QLDPIYVDVT QSTAELLKLR RDLESGQLQK AGDNAASVQL VLEDGSLFKQ
     EGRLEFSEVA VDETTGSVTL RALFPNPDHT LLPGMFVHAR LKAGVNANAI LAPQQGVTRD
     LKGAPTALVV NQENKVELRQ LKASRTLGSD WLIEEGLNPG DRLITEGLQY VRPGVEVKVS
     DATNVKKPAG PDQANAAKAD AKAE