ID   ARPA_PSEPU              Reviewed;         371 AA.
AC   Q9KJC3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Antibiotic efflux pump periplasmic linker protein ArpA;
DE   Flags: Precursor;
GN   Name=arpA;
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 periplasmic linker protein component of an antibiotic
CC       efflux pump. Confers resistance to numerous structurally unrelated
CC       antibiotics such as carbenicillin, chloramphenicol, erythromycin,
CC       novobiocin, streptomycin and tetracycline. Is not involved in organic
CC       solvent efflux.
CC   -!- SUBCELLULAR LOCATION: Cell inner 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 membrane fusion protein (MFP) (TC 8.A.1)
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; AAF73831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJC3; -.
DR   SMR; Q9KJC3; -.
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   2: Evidence at transcript 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..371
FT                   /note="Antibiotic efflux pump periplasmic linker protein
FT                   ArpA"
FT                   /id="PRO_0000018689"
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   371 AA;  40277 MW;  B86AACE9A6133645 CRC64;
     MQFKPAVTAL VSAVALATLL SGCKKEEAAP AAQAPQVGVV TIQPQAFTLT SELPGRTSAY
     RVAEVRPQVN GIILKRLFKE GSEVKEGQQL YQIDPAVYEA TLANAKANLL ATRSLAERYK
     QLIDEQAVSK QEYDDANAKR LQAEASLKSA QIDLRYTKVL APISGRIGRS SFTEGALVSN
     GQTDAMATIQ QLDPIYVDVT QSTAELLKLR RDLESGQLQK AGNNAASVQL VLEDGSLFKQ
     EGRLEFSEVA VDETTGSVTL RALFPNPDHT LLPGMFVHAR LKAGVNANAI LAPQQGVTRD
     LKGAPTALVV NQENKVELRQ LKASRTLGSD WLIEEGLNPG DRLITEGLQY VSPRRRGEGQ
     RCHQRQEAGR P