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GLUA_CORGL
ID   GLUA_CORGL              Reviewed;         242 AA.
AC   P48243;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Glutamate transport ATP-binding protein GluA {ECO:0000305};
DE            EC=7.4.2.1 {ECO:0000305|PubMed:7868586};
DE   AltName: Full=Glutamate uptake system protein GluA {ECO:0000305};
GN   Name=gluA {ECO:0000303|PubMed:7868586}; OrderedLocusNames=Cgl1950, cg2136;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=7868586; DOI=10.1128/jb.177.5.1152-1158.1995;
RA   Kronemeyer W., Peekhaus N., Kraemer R., Sahm H., Eggeling L.;
RT   "Structure of the gluABCD cluster encoding the glutamate uptake system of
RT   Corynebacterium glutamicum.";
RL   J. Bacteriol. 177:1152-1158(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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:0000269|PubMed:7868586}.
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:0000305|PubMed:7868586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674;
CC         Evidence={ECO:0000305|PubMed:7868586};
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:0000305|PubMed:7868586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29036;
CC         Evidence={ECO:0000305|PubMed:7868586};
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:0000305|PubMed:7868586}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gluABCD cluster almost abolishes
CC       glutamate uptake activity. {ECO:0000269|PubMed:7868586}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; X81191; CAA57060.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99343.1; -; Genomic_DNA.
DR   EMBL; BX927153; CAF20291.1; -; Genomic_DNA.
DR   RefSeq; NP_601157.1; NC_003450.3.
DR   AlphaFoldDB; P48243; -.
DR   SMR; P48243; -.
DR   STRING; 196627.cg2136; -.
DR   TCDB; 3.A.1.3.9; the atp-binding cassette (abc) superfamily.
DR   KEGG; cgb:cg2136; -.
DR   KEGG; cgl:Cgl1950; -.
DR   PATRIC; fig|196627.13.peg.1888; -.
DR   eggNOG; COG1126; Bacteria.
DR   HOGENOM; CLU_000604_1_22_11; -.
DR   OMA; APIWVRR; -.
DR   Proteomes; UP000000582; 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   1: Evidence at protein level;
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_0000092338"
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"
FT   CONFLICT        149
FT                   /note="R -> C (in Ref. 1; CAA57060)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  26538 MW;  94401A263DE00194 CRC64;
     MIKMTGVQKY FGDFHALTDI DLEIPRGQVV VVLGPSGSGK STLCRTINRL ETIEEGTIEI
     DGKVLPEEGK GLANLRADVG MVFQSFNLFP HLTIKDNVTL APIKVRKMKK SEAEKLAMSL
     LERVGIANQA DKYPAQLSGG QQQRVAIARA LAMNPKIMLF DEPTSALDPE MVNEVLDVMA
     SLAKEGMTMV CVTHEMGFAR KAADRVLFMA DGLIVEDTEP DSFFTNPKSD RAKDFLGKIL
     AH
 
 
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