DGAL_CITFR
ID DGAL_CITFR Reviewed; 332 AA.
AC P23925;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=D-galactose-binding periplasmic protein;
DE Short=GBP;
DE AltName: Full=D-galactose/ D-glucose-binding protein;
DE Short=GGBP;
DE Flags: Precursor;
GN Name=mglB;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750;
RA Galindo R.L., Daggett Garvin L., Hardies S.C.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is involved in the active transport of galactose
CC and glucose. It plays a role in the chemotaxis towards the two sugars
CC by interacting with the trg chemoreceptor.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DOMAIN: The calcium-binding site is structurally similar to that of EF-
CC hand proteins, but is in two parts, with the last calcium ligand
CC provided by Glu-228.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X59389; CAA42032.1; -; Genomic_DNA.
DR PIR; S15554; S15554.
DR RefSeq; WP_003027399.1; NZ_VTEC01000008.1.
DR AlphaFoldDB; P23925; -.
DR SMR; P23925; -.
DR STRING; 1333848.CFNIH1_22040; -.
DR PRIDE; P23925; -.
DR GeneID; 61127696; -.
DR GeneID; 64169392; -.
DR GeneID; 67515925; -.
DR OrthoDB; 1378040at2; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd01539; PBP1_GGBP; 1.
DR InterPro; IPR044085; MglB-like_PBP1.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 3: Inferred from homology;
KW Calcium; Chemotaxis; Metal-binding; Periplasm; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..23
FT CHAIN 24..332
FT /note="D-galactose-binding periplasmic protein"
FT /id="PRO_0000031721"
FT BINDING 37
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 37
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 114
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 114
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 175
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 175
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 177
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 177
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 181
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 181
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 234
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 234
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 259
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 259
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 279
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:P23905"
FT BINDING 279
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT SITE 97
FT /note="Interacts with membrane-bound trg signal transducer"
SQ SEQUENCE 332 AA; 35817 MW; 2530E7EDE0471B1B CRC64;
MNKKVLTLSA VMASMLFGAA AHAADTRIGV TIYKYDDNFM SVVRKAIEKD AKAAPDVQLL
MNDSQNDQSK QNDQIDVLLA KGVKALAINL VDPAAAGTVI EKARGQNVPI VFFNKEPSRK
ALDSYDKAYY VGTDSKESGI IQGDLIAKHW AANPNWDLNK DGKIQFVLLK GEPGHPDAEA
RTTYVIKELN DKGIKTEQLQ LDTAMWDTAQ AKDKMDAWMS GPNANKIEVV IANNDAMAMG
AVEALKAHNK TSVPVFGVDA LPEALALVKS GAMAGTVLND ANNQAKATFD LAKNLADGKG
AADGTNWKIE NKIVRVPYVG VDKDNLAEFT NK
