DGAL_SALTY
ID DGAL_SALTY Reviewed; 332 AA.
AC P23905;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=STM2190;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3146019; DOI=10.1007/bf00330498;
RA Benner-Luger D., Boos W.;
RT "The mglB sequence of Salmonella typhimurium LT2; promoter analysis by gene
RT fusions and evidence for a divergently oriented gene coding for the mgl
RT repressor.";
RL Mol. Gen. Genet. 214:579-587(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=6345536; DOI=10.2210/pdb1gbp/pdb;
RA Mowbray S.L., Petsko G.A.;
RT "The X-ray structure of the periplasmic galactose binding protein from
RT Salmonella typhimurium at 3.0-A resolution.";
RL J. Biol. Chem. 258:7991-7997(1983).
RN [4] {ECO:0007744|PDB:1GCA}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-332 IN COMPLEX WITH CALCIUM AND
RP BETA-D-GALACTOSE.
RX PubMed=8240551; DOI=10.1006/jmbi.1993.1549;
RA Zhou J.Y., Flocco M.M., Mowbray S.L.;
RT "The 1.7 A refined X-ray structure of the periplasmic glucose/galactose
RT receptor from Salmonella typhimurium.";
RL J. Mol. Biol. 233:739-752(1993).
RN [5] {ECO:0007744|PDB:1GCG}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-332 IN COMPLEX WITH CALCIUM.
RX PubMed=8132630; DOI=10.1016/s0021-9258(17)37057-6;
RA Flocco M.M., Mowbray S.L.;
RT "The 1.9 A X-ray structure of a closed unliganded form of the periplasmic
RT glucose/galactose receptor from Salmonella typhimurium.";
RL J. Biol. Chem. 269:8931-8936(1994).
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; AE006468; AAL21094.1; -; Genomic_DNA.
DR PIR; S29390; S29390.
DR RefSeq; NP_461135.1; NC_003197.2.
DR RefSeq; WP_001036943.1; NC_003197.2.
DR PDB; 1GCA; X-ray; 1.70 A; A=24-332.
DR PDB; 1GCG; X-ray; 1.90 A; A=24-332.
DR PDB; 3GA5; X-ray; 1.87 A; A/B=24-332.
DR PDB; 3GBP; X-ray; 2.40 A; A=24-330.
DR PDBsum; 1GCA; -.
DR PDBsum; 1GCG; -.
DR PDBsum; 3GA5; -.
DR PDBsum; 3GBP; -.
DR AlphaFoldDB; P23905; -.
DR SMR; P23905; -.
DR STRING; 99287.STM2190; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR PaxDb; P23905; -.
DR EnsemblBacteria; AAL21094; AAL21094; STM2190.
DR GeneID; 1253712; -.
DR KEGG; stm:STM2190; -.
DR PATRIC; fig|99287.12.peg.2317; -.
DR HOGENOM; CLU_037628_3_1_6; -.
DR OMA; MWDAAMA; -.
DR PhylomeDB; P23905; -.
DR BioCyc; SENT99287:STM2190-MON; -.
DR EvolutionaryTrace; P23905; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Chemotaxis; Metal-binding; Periplasm;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..23
FT CHAIN 24..332
FT /note="D-galactose-binding periplasmic protein"
FT /id="PRO_0000031723"
FT BINDING 37
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 175
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8132630,
FT ECO:0000269|PubMed:8240551, ECO:0007744|PDB:1GCA,
FT ECO:0007744|PDB:1GCG"
FT BINDING 234
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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:0000269|PubMed:8240551,
FT ECO:0007744|PDB:1GCA"
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 CONFLICT 175
FT /note="H -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:1GCA"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1GCA"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1GCA"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1GCA"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1GCA"
SQ SEQUENCE 332 AA; 35814 MW; CF31E994E00992D2 CRC64;
MNKKVLTLSA VMASLLFGAH AHAADTRIGV TIYKYDDNFM SVVRKAIEKD GKSAPDVQLL
MNDSQNDQSK QNDQIDVLLA KGVKALAINL VDPAAAGTVI EKARGQNVPV VFFNKEPSRK
ALDSYDKAYY VGTDSKESGV IQGDLIAKHW QANQGWDLNK DGKIQYVLLK GEPGHPDAEA
RTTYVVKELN DKGIQTEQLA LDTAMWDTAQ AKDKMDAWLS GPNANKIEVV IANNDAMAMG
AVEALKAHNK SSIPVFGVDA LPEALALVKS GAMAGTVLND ANNQAKATFD LAKNLAEGKG
AADGTSWKIE NKIVRVPYVG VDKDNLSEFT QK
