DGAL_SHIFL
ID DGAL_SHIFL Reviewed; 332 AA.
AC P0AEE7; P02927; P17775;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; OrderedLocusNames=SF2235, S2364;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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. {ECO:0000250}.
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; AE005674; AAN43756.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17573.1; -; Genomic_DNA.
DR RefSeq; NP_708049.1; NC_004337.2.
DR RefSeq; WP_001036964.1; NZ_WPGW01000017.1.
DR AlphaFoldDB; P0AEE7; -.
DR BMRB; P0AEE7; -.
DR SMR; P0AEE7; -.
DR STRING; 198214.SF2235; -.
DR PRIDE; P0AEE7; -.
DR EnsemblBacteria; AAN43756; AAN43756; SF2235.
DR EnsemblBacteria; AAP17573; AAP17573; S2364.
DR GeneID; 1027319; -.
DR GeneID; 66673954; -.
DR KEGG; sfl:SF2235; -.
DR KEGG; sfx:S2364; -.
DR PATRIC; fig|198214.7.peg.2677; -.
DR HOGENOM; CLU_037628_3_1_6; -.
DR OMA; MWDAAMA; -.
DR OrthoDB; 1378040at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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; Reference proteome; Signal;
KW Sugar transport; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..332
FT /note="D-galactose-binding periplasmic protein"
FT /id="PRO_0000043345"
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:P0AEE5"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0AEE5"
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:P0AEE5"
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"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 35713 MW; 9A57E86C423AA6D3 CRC64;
MNKKVLTLSA VMASMLFGAA AHAADTRIGV TIYKYDDNFM SVVRKAIEQD AKAAPDVQLL
MNDSQNDQSK QNDQIDVLLA KGVKALAINL VDPAAAGTVI EKARGQNVPV VFFNKEPSRK
ALDSYDKAYY VGTDSKESGI IQGDLIAKHW AANQGWDLNK DGQIQFVLLK GEPGHPDAEA
RTTYVIKELN DKGIKTEQLQ LDTAMWDTAQ AKDKMDAWLS GPNANKIEVV IANNDAMAMG
AVEALKAHNK SSIPVFGVDA LPEALALVKS GALAGTVLND ANNQAKATFD LAKNLADGKG
AADGTNWKID NKVVRVPYVG VDKDNLAEFS KK
