ID   ARTP_ECOL6              Reviewed;         242 AA.
AC   P0AAF7; P30858; P77355;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Arginine transport ATP-binding protein ArtP;
DE            EC=7.4.2.-;
GN   Name=artP; OrderedLocusNames=c0997;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in
CC       arginine transport. Probably responsible for energy coupling to the
CC       transport system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ArtP),
CC       two transmembrane proteins (ArtM and ArtQ) and two solute-binding
CC       proteins (ArtJ and ArtI). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79470.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000027205.1; NC_004431.1.
DR   AlphaFoldDB; P0AAF7; -.
DR   SMR; P0AAF7; -.
DR   STRING; 199310.c0997; -.
DR   EnsemblBacteria; AAN79470; AAN79470; c0997.
DR   GeneID; 66670862; -.
DR   KEGG; ecc:c0997; -.
DR   eggNOG; COG1126; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; DMVPCEL; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..242
FT                   /note="Arginine transport ATP-binding protein ArtP"
FT                   /id="PRO_0000091941"
FT   DOMAIN          3..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   242 AA;  27022 MW;  D5B50062E523413A CRC64;
     MSIQLNGINC FYGAHQALFD ITLDCPQGET LVLLGPSGAG KSSLLRVLNL LEMPRSGTLN
     IAGNHFDFTK TPSDKAIRDL RRNVGMVFQQ YNLWPHLTVQ QNLIEAPCRV LGLSKDQALA
     RAEKLLERLR LKPYSDRYPL HLSGGQQQRV AIARALMMEP QVLLFDEPTA ALDPEITAQI
     VSIIRELAET NITQVIVTHE VEVARKTASR VVYMENGHIV EQGDASCFTE PQTEAFKNYL
     SH