ID MGLB_CITFR Reviewed; 332 AA. AC P23925; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 02-OCT-2024, entry version 99. DE RecName: Full=D-galactose/methyl-galactoside binding periplasmic protein MglB {ECO:0000250|UniProtKB:P0AEE5}; DE AltName: 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; Pseudomonadota; 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: Part of the ABC transporter complex MglABC involved in CC galactose/methyl galactoside import (By similarity). In addition, binds CC D-galactose and D-glucose and plays a role in the chemotaxis towards CC these two sugars by interacting with the Trg chemoreceptor (By CC similarity). {ECO:0000250|UniProtKB:P0AEE5}. CC -!- SUBUNIT: The ABC transporter complex is composed of one ATP-binding CC protein (MglA), two transmembrane proteins (MglC) and a solute-binding CC protein (MglB). {ECO:0000250|UniProtKB:P0AEE5}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59389; CAA42032.1; -; Genomic_DNA. DR PIR; S15554; S15554. DR RefSeq; WP_003027399.1; NZ_VWTQ01000002.1. DR AlphaFoldDB; P23925; -. DR SMR; P23925; -. DR STRING; 1333848.CFNIH1_22040; -. DR GeneID; 87000510; -. DR OrthoDB; 9769193at2; -. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR CDD; cd01539; PBP1_GGBP; 1. DR Gene3D; 3.40.50.2300; -; 2. DR InterPro; IPR050555; Bact_Solute-Bind_Prot2. DR InterPro; IPR044085; MglB-like_PBP1. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR PANTHER; PTHR30036:SF2; D-GALACTOSE-BINDING PERIPLASMIC PROTEIN; 1. DR PANTHER; PTHR30036; D-XYLOSE-BINDING PERIPLASMIC PROTEIN; 1. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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/methyl-galactoside binding periplasmic FT protein MglB" 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 //