ARTP_ECO57
ID ARTP_ECO57 Reviewed; 242 AA.
AC P0AAF8; P30858; P77355;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Arginine transport ATP-binding protein ArtP;
DE EC=7.4.2.-;
GN Name=artP; OrderedLocusNames=Z1094, ECs0947;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG55243.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34370.1; -; Genomic_DNA.
DR PIR; C90747; C90747.
DR PIR; G85597; G85597.
DR RefSeq; NP_308974.1; NC_002695.1.
DR RefSeq; WP_000027205.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AAF8; -.
DR SMR; P0AAF8; -.
DR STRING; 155864.EDL933_0997; -.
DR PRIDE; P0AAF8; -.
DR EnsemblBacteria; AAG55243; AAG55243; Z1094.
DR EnsemblBacteria; BAB34370; BAB34370; ECs_0947.
DR GeneID; 66670862; -.
DR GeneID; 917689; -.
DR KEGG; ece:Z1094; -.
DR KEGG; ecs:ECs_0947; -.
DR PATRIC; fig|386585.9.peg.1065; -.
DR eggNOG; COG1126; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; ATMLKPN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Translocase; Transport.
FT CHAIN 1..242
FT /note="Arginine transport ATP-binding protein ArtP"
FT /id="PRO_0000091940"
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