ID   ARTP_ECOLI              Reviewed;         242 AA.
AC   P0AAF6; P30858; P77355;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   02-SEP-2026, entry version 140.
DE   RecName: Full=Arginine transport ATP-binding protein ArtP {ECO:0000305};
DE            EC=7.4.2.1 {ECO:0000305|PubMed:8801422};
GN   Name=artP {ECO:0000303|PubMed:8501075};
GN   OrderedLocusNames=b0864, JW0848;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / AN387;
RX   PubMed=8501075; DOI=10.1128/jb.175.11.3687-3688.1993;
RA   Wissenbach U., Unden G.;
RT   "Physical map location of the new artPIQMJ genes of Escherichia coli,
RT   encoding a periplasmic arginine transport system.";
RL   J. Bacteriol. 175:3687-3688(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=8801422; DOI=10.1111/j.1365-2958.1995.mmi_17040675.x;
RA   Wissenbach U., Six S., Bongaerts J., Ternes D., Steinwachs S., Unden G.;
RT   "A third periplasmic transport system for L-arginine in Escherichia coli:
RT   molecular characterization of the artPIQMJ genes, arginine binding and
RT   transport.";
RL   Mol. Microbiol. 17:675-686(1995).
CC   -!- FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in
CC       arginine transport. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000269|PubMed:8801422}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a polar amino acid(out) + ATP + H2O = a polar amino acid(in) +
CC         ADP + phosphate + H(+); Xref=Rhea:RHEA:14673, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:62031, ChEBI:CHEBI:456216; EC=7.4.2.1;
CC         Evidence={ECO:0000305|PubMed:8801422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674;
CC         Evidence={ECO:0000305|PubMed:8801422};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(out) + ATP + H2O = L-arginine(in) + ADP + phosphate
CC         + H(+); Xref=Rhea:RHEA:29879, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.4.2.1;
CC         Evidence={ECO:0000305|PubMed:8801422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29880;
CC         Evidence={ECO:0000305|PubMed:8801422};
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:0000305|PubMed:8801422}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; X86160; CAA60101.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73951.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35578.1; -; Genomic_DNA.
DR   PIR; H64824; H64824.
DR   RefSeq; NP_415385.1; NC_000913.3.
DR   RefSeq; WP_000027205.1; NZ_CP009789.1.
DR   AlphaFoldDB; P0AAF6; -.
DR   SMR; P0AAF6; -.
DR   BioGRID; 4263133; 14.
DR   BioGRID; 849863; 6.
DR   ComplexPortal; CPX-4318; Arginine ABC transporter complex, artI variant.
DR   ComplexPortal; CPX-4319; Arginine ABC transporter complex, artJ variant.
DR   DIP; DIP-47917N; -.
DR   FunCoup; P0AAF6; 359.
DR   IntAct; P0AAF6; 12.
DR   STRING; 511145.b0864; -.
DR   TCDB; 3.A.1.3.3; the atp-binding cassette (abc) superfamily.
DR   jPOST; P0AAF6; -.
DR   PaxDb; 511145-b0864; -.
DR   EnsemblBacteria; AAC73951; AAC73951; b0864.
DR   GeneID; 86945751; -.
DR   GeneID; 93776558; -.
DR   GeneID; 945489; -.
DR   KEGG; ecj:JW0848; -.
DR   KEGG; eco:b0864; -.
DR   KEGG; ecoc:C3026_05380; -.
DR   PATRIC; fig|1411691.4.peg.1413; -.
DR   EchoBASE; EB1581; -.
DR   eggNOG; COG1126; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   InParanoid; P0AAF6; -.
DR   OMA; YMEQGHI; -.
DR   OrthoDB; 9802264at2; -.
DR   PhylomeDB; P0AAF6; -.
DR   BioCyc; EcoCyc:ARTP-MONOMER; -.
DR   BioCyc; MetaCyc:ARTP-MONOMER; -.
DR   PRO; PR:P0AAF6; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AAF6; -.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; ISO:EcoCyc.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015426; F:ATPase-coupled polar amino acid-transporter activity; ISM:EcoCyc.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:EcoCyc.
DR   FunFam; 3.40.50.300:FF:000331; Arginine ABC transporter ATP-binding protein ArtP; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR050086; MetN_ABC_transporter-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF008338; PRK11124.1; 1.
DR   PANTHER; PTHR43166; AMINO ACID IMPORT ATP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR43166:SF25; ARGININE TRANSPORT ATP-BINDING PROTEIN ARTP; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..242
FT                   /note="Arginine transport ATP-binding protein ArtP"
FT                   /id="PRO_0000091939"
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"
FT   CONFLICT        94..95
FT                   /note="WP -> CA (in Ref. 1; CAA60101)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="R -> S (in Ref. 1; CAA60101)"
FT                   /evidence="ECO:0000305"
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
//