GLUB_CORGL
ID GLUB_CORGL Reviewed; 295 AA.
AC P48242;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glutamate-binding protein GluB {ECO:0000303|PubMed:32593757};
DE AltName: Full=Glutamate uptake system protein GluB {ECO:0000305};
DE Flags: Precursor;
GN Name=gluB {ECO:0000303|PubMed:7868586}; OrderedLocusNames=Cgl1951, cg2137;
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).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=32593757; DOI=10.1016/j.ijbiomac.2020.06.197;
RA Capo A., Natalello A., Marienhagen J., Pennacchio A., Camarca A.,
RA Di Giovanni S., Staiano M., D'Auria S., Varriale A.;
RT "Structural features of the glutamate-binding protein from Corynebacterium
RT glutamicum.";
RL Int. J. Biol. Macromol. 162:903-912(2020).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=23722846; DOI=10.1107/s1744309113011652;
RA Liu Q., Li D., Hu Y., Wang D.-C.;
RT "Expression, crystallization and preliminary crystallographic study of GluB
RT from Corynebacterium glutamicum.";
RL Acta Crystallogr. F 69:657-659(2013).
CC -!- FUNCTION: Part of the ABC transporter complex GluABCD involved in
CC glutamate uptake (PubMed:7868586). Binds glutamate with a high affinity
CC (PubMed:32593757). Also binds aspartate with high affinity, suggesting
CC that GluB could be involved in the transport of both amino acid
CC residues into the cell (PubMed:32593757). {ECO:0000269|PubMed:32593757,
CC ECO:0000269|PubMed:7868586}.
CC -!- ACTIVITY REGULATION: Binding of glutamate or asparatate induces a
CC higher thermal stability of the protein structure.
CC {ECO:0000269|PubMed:32593757}.
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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gluABCD cluster almost abolishes
CC glutamate uptake activity. {ECO:0000269|PubMed:7868586}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; X81191; CAA57061.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99344.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20292.1; -; Genomic_DNA.
DR RefSeq; NP_601158.1; NC_003450.3.
DR RefSeq; WP_011014779.1; NC_006958.1.
DR AlphaFoldDB; P48242; -.
DR SMR; P48242; -.
DR STRING; 196627.cg2137; -.
DR TCDB; 3.A.1.3.9; the atp-binding cassette (abc) superfamily.
DR KEGG; cgb:cg2137; -.
DR KEGG; cgl:Cgl1951; -.
DR PATRIC; fig|196627.13.peg.1889; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_4_11; -.
DR OMA; IFATYSI; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 27..295
FT /note="Glutamate-binding protein GluB"
FT /id="PRO_0000031761"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 295 AA; 31668 MW; 164384D11D6B1378 CRC64;
MSAKRTFTRI GAILGATALA GVTLTACGDS SGGDGFLAAI ENGSVNVGTK YDQPGLGLRN
PDNSMSGLDV DVAEYVVNSI ADDKGWDHPT IEWRESPSAQ RETLIQNGEV DMIAATYSIN
AGRSESVNFG GPYLLTHQAL LVRQDDDRIE TLEDLDNGLI LCSVSGSTPA QKVKDVLPGV
QLQEYDTYSS CVEALSQGNV DALTTDATIL FGYSQQYEGD FRVVEMEKDG EPFTDEYYGI
GLKKDDQEGT DAINAALERM YADGTFQRLL TENLGEDSVV VEEGTPGDLS FLDAS
