ID   MEPC_PSEPU              Reviewed;         484 AA.
AC   P0C071;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Multidrug/solvent efflux pump outer membrane protein MepC;
DE   Flags: Precursor;
GN   Name=mepC;
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 outer membrane component of an organic solvent and
CC       antibiotic efflux pump; confers resistance to toluene, hexane, p-
CC       xylene, ampicillin, penicillin G, erythromycin, novobiocin and
CC       tetracycline.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
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_010952492.1; NZ_PZKR01000020.1.
DR   AlphaFoldDB; P0C071; -.
DR   SMR; P0C071; -.
DR   STRING; 1240350.AMZE01000001_gene2849; -.
DR   PRIDE; P0C071; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR003423; OMP_efflux.
DR   InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
DR   Pfam; PF02321; OEP; 2.
DR   TIGRFAMs; TIGR01845; outer_NodT; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell outer membrane; Lipoprotein; Membrane;
KW   Palmitate; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..484
FT                   /note="Multidrug/solvent efflux pump outer membrane protein
FT                   MepC"
FT                   /id="PRO_0000031004"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   484 AA;  52864 MW;  FFD6E78FBC55C678 CRC64;
     MTKSLLSLAV TAFILGGCSL IPDYQTPEAP VAAQWPQGPA YSPTQSADVA AAEQGWRQFF
     HDPALQQLIQ TSLVNNRDLR VAALNLDAYR AQYRIQRADL FPAVSATGSG SRQRVPANMS
     QTGESGITSQ YSATLGVSAY ELDLFGRVRS LTEQALETYL SSEQARRSTQ IALVASVANA
     YYTWQADQAL FKLTEETLKT YEESYNLTRR SNEVGVASAL DVSQARTAVE GARVKYSQYQ
     RLVAQDVNSL TVLLGTGIPA DLAKPLELDA DQLAEVPAGL PSDILQRRPD IQEAEHLLKA
     ANANIGAARA AFFPSISLTA NAGSLSPDMG HLFSGGQGTW LFQPQINLPI FNAGSLKASL
     DYSKIQKDIN VAKYEKTIQT AFQEVSDGLA ARKTFEEQLQ AQRDLVQANQ DYYRLAERRY
     RIGIDSNLTF LDAQRNLFSA QQALIGDRLS QLTSEVNLYK ALGGGWYEQT GQANQQASVE
     TPKG