GLUB_COREF
ID GLUB_COREF Reviewed; 294 AA.
AC Q8RQL6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Glutamate-binding protein GluB {ECO:0000250|UniProtKB:P48242};
DE Flags: Precursor;
GN Name=gluB {ECO:0000303|Ref.1}; OrderedLocusNames=CE1845;
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 (By similarity). Binds glutamate with a high affinity
CC (By similarity). {ECO:0000250|UniProtKB:P48242}.
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:P48242}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; AB083297; BAB88899.1; -; Genomic_DNA.
DR EMBL; BA000035; BAC18655.1; -; Genomic_DNA.
DR RefSeq; WP_011075640.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8RQL6; -.
DR SMR; Q8RQL6; -.
DR STRING; 196164.23493686; -.
DR EnsemblBacteria; BAC18655; BAC18655; BAC18655.
DR KEGG; cef:CE1845; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_4_11; -.
DR OMA; IFATYSI; -.
DR OrthoDB; 685252at2; -.
DR Proteomes; UP000001409; 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 3: Inferred from homology;
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..294
FT /note="Glutamate-binding protein GluB"
FT /id="PRO_0000031760"
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 294 AA; 31815 MW; A32E900BB6952DC0 CRC64;
MSHKRMFTRL AAATSAAVLA GITLTACGDS EGGDGLLAAI ENGNVTIGTK YDQPGLGLRN
PDNSMSGLDV DVAQYVVNSI ADDNGWDHPT VEWRETPSAQ RETLIQNGEV DMIAATYSIN
PGRSESVNFG GPYLLTHQAL LVREDDDRIQ TLEDLDDGLI LCSVTGSTPA QKVKDVLPGV
QLQEYDTYSS CVEALSQGNV DAMTTDATIL FGYAQQREGE FRVVEMEQDG EPFTNEYYGI
GITKDDTEAT DAINAALERM YADGSFQRFL TENLGEDSQV VQEGTPGDLS FLDE
