ID   GLUA_COREF              Reviewed;         242 AA.
AC   Q8RQL7;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Glutamate transport ATP-binding protein GluA {ECO:0000250|UniProtKB:P48243};
DE            EC=7.4.2.1 {ECO:0000250|UniProtKB:P48243};
GN   Name=gluA {ECO:0000303|Ref.1}; OrderedLocusNames=CE1844;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA   Nonaka G., Kimura E., Kawahara Y., Sugimoto S.;
RT   "Corynebacterium efficiens gluA, gluB, gluC and gluD genes, complete CDS.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex GluABCD involved in
CC       glutamate uptake. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000250|UniProtKB:P48243}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a polar amino acid(out) + ATP + H2O = a polar amino acid(in) +
CC         ADP + H(+) + phosphate; 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:0000250|UniProtKB:P48243};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674;
CC         Evidence={ECO:0000250|UniProtKB:P48243};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamate(out) = ADP + H(+) + L-glutamate(in) +
CC         phosphate; Xref=Rhea:RHEA:29035, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P48243};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29036;
CC         Evidence={ECO:0000250|UniProtKB:P48243};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GluA),
CC       two transmembrane proteins (GluC and GluD) and a solute-binding protein
CC       (GluB). {ECO:0000250|UniProtKB:P48243}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48243};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P48243}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC18654.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB083297; BAB88898.1; -; Genomic_DNA.
DR   EMBL; BA000035; BAC18654.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8RQL7; -.
DR   SMR; Q8RQL7; -.
DR   STRING; 196164.23493685; -.
DR   EnsemblBacteria; BAC18654; BAC18654; BAC18654.
DR   KEGG; cef:CE1844; -.
DR   eggNOG; COG1126; Bacteria.
DR   HOGENOM; CLU_000604_1_22_11; -.
DR   Proteomes; UP000001409; 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 membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..242
FT                   /note="Glutamate transport ATP-binding protein GluA"
FT                   /id="PRO_0000092337"
FT   DOMAIN          2..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   242 AA;  26604 MW;  AFBCAA2D7D36BB69 CRC64;
     MIKMTGVQKF FDDFQALTDI NLEVPAGQVV VVLGPSGSGK STLCRTINRL ETIEEGTIEI
     DGKLLPEEGK DLAKIRADVG MVFQSFNLFP HLTIKDNVTL GPMKVRKMKK SEANEVAMKL
     LERVGIANQA EKYPAQLSGG QQQRVAIARA LAMNPKIMLF DEPTSALDPE MVNEVLDVMA
     SLAKEGMTMV CVTHEMGFAR RAADRVLFMS DGAIVEDSDP ETFFTNPQTD RAKDFLGKIL
     AH