ID   ARPC_PSEPU              Reviewed;         484 AA.
AC   Q9KJC1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Antibiotic efflux pump outer membrane protein ArpC;
DE   Flags: Precursor;
GN   Name=arpC;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], EFFLUX PUMP SUBSTRATES, AND INDUCTION.
RC   STRAIN=ATCC 700801 / S12;
RX   PubMed=11160799; DOI=10.1099/00221287-147-1-43;
RA   Kieboom J., de Bont J.A.M.;
RT   "Identification and molecular characterization of an efflux system involved
RT   in Pseudomonas putida S12 multidrug resistance.";
RL   Microbiology 147:43-51(2001).
CC   -!- FUNCTION: The outer membrane component of an antibiotic efflux pump.
CC       Confers resistance to numerous structurally unrelated antibiotics such
CC       as carbenicillin, chloramphenicol, erythromycin, novobiocin,
CC       streptomycin and tetracycline. Is not involved in organic solvent
CC       efflux.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: The arpABC operon was not seen to be induced by
CC       carbenicillin, chloramphenicol, erythromycin nor by hexane, toluene or
CC       p-xylene. {ECO:0000269|PubMed:11160799}.
CC   -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Despite being nearly identical to the ttgABC operon in strain
CC       DOT-T1E and the mepABC operon in strain KT2442-TOL this operon does not
CC       function in solvent efflux. This may be due to different protein
CC       expression levels. In strain KT2440 the equivalent operon does not seem
CC       to function in toluene efflux. {ECO:0000305}.
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DR   EMBL; AF183959; AAF73833.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJC1; -.
DR   SMR; Q9KJC1; -.
DR   eggNOG; COG1538; Bacteria.
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   2: Evidence at transcript 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="Antibiotic efflux pump outer membrane protein ArpC"
FT                   /id="PRO_0000031003"
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;  52834 MW;  9AE1A851FB0B092E CRC64;
     MTKSLLSLAV TAFILGGCSL IPDYQAPEAP 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