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   02-SEP-2026, entry version 115.
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; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; 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; NC_004369.1.
DR   AlphaFoldDB; Q8RQL6; -.
DR   SMR; Q8RQL6; -.
DR   STRING; 196164.gene:10742273; -.
DR   KEGG; cef:CE1845; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_4_11; -.
DR   OrthoDB; 9807888at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006865; P:amino acid transport; IEA:TreeGrafter.
DR   CDD; cd13690; PBP2_GluB; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR051455; Bact_solute-bind_prot3.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR30085:SF6; ABC TRANSPORTER GLUTAMINE-BINDING PROTEIN GLNH; 1.
DR   PANTHER; PTHR30085; AMINO ACID ABC TRANSPORTER PERMEASE; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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
//