DGAL_ECOLI
ID DGAL_ECOLI Reviewed; 332 AA.
AC P0AEE5; P02927; P17775; Q2MAS9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=b2150, JW2137;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1719366; DOI=10.1007/bf00267469;
RA Hogg R.W., Voelker C., von Carlowitz I.;
RT "Nucleotide sequence and analysis of the mgl operon of Escherichia coli
RT K12.";
RL Mol. Gen. Genet. 229:453-459(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-74.
RC STRAIN=K12;
RX PubMed=3302609; DOI=10.1007/bf00330450;
RA Scholle A., Vreemann J., Blank V., Nold A., Boos W., Manson M.D.;
RT "Sequence of the mglB gene from Escherichia coli K12: comparison of wild-
RT type and mutant galactose chemoreceptors.";
RL Mol. Gen. Genet. 208:247-253(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 24-332.
RX PubMed=7012152; DOI=10.1016/s0021-9258(19)69441-x;
RA Mahoney W.C., Hogg R.W., Hermodson M.A.;
RT "The amino acid sequence of the D-galactose-binding protein from
RT Escherichia coli B/r.";
RL J. Biol. Chem. 256:4350-4356(1981).
RN [7]
RP SEQUENCE REVISION TO 179-180.
RA Mahoney W.C., Hogg R.W., Hermodson M.A.;
RL Submitted (NOV-1982) to the PIR data bank.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX PubMed=6885805; DOI=10.1016/s0021-9258(17)44353-5;
RA Scripture J.B., Hogg R.W.;
RT "The nucleotide sequences defining the signal peptides of the galactose-
RT binding protein and the arabinose-binding protein.";
RL J. Biol. Chem. 258:10853-10855(1983).
RN [9]
RP PROTEIN SEQUENCE OF 24-47.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=6340108; DOI=10.1073/pnas.80.7.1792;
RA Vyas N.K., Vyas M.N., Quiocho F.A.;
RT "The 3-A resolution structure of a D-galactose-binding protein for
RT transport and chemotaxis in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:1792-1796(1983).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RX PubMed=3600760; DOI=10.1038/327635a0;
RA Vyas N.K., Vyas M.N., Quiocho F.A.;
RT "A novel calcium binding site in the galactose-binding protein of bacterial
RT transport and chemotaxis.";
RL Nature 327:635-638(1987).
RN [13] {ECO:0007744|PDB:2GBP}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-332 IN COMPLEX WITH CALCIUM AND
RP BETA-D-GLUCOSE.
RX PubMed=3057628; DOI=10.1126/science.3057628;
RA Vyas N.K., Vyas M.N., Quiocho F.A.;
RT "Sugar and signal-transducer binding sites of the Escherichia coli
RT galactose chemoreceptor protein.";
RL Science 242:1290-1295(1988).
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; M59444; AAA24169.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60523.1; -; Genomic_DNA.
DR EMBL; X05646; CAA29132.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75211.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76627.1; -; Genomic_DNA.
DR EMBL; K00419; AAA24172.1; -; Genomic_DNA.
DR PIR; A37277; JGECG.
DR RefSeq; NP_416655.1; NC_000913.3.
DR RefSeq; WP_001036964.1; NZ_STEB01000002.1.
DR PDB; 1GLG; X-ray; 2.00 A; A=24-332.
DR PDB; 2FVY; X-ray; 0.92 A; A=24-332.
DR PDB; 2FW0; X-ray; 1.55 A; A=24-332.
DR PDB; 2GBP; X-ray; 1.90 A; A=24-332.
DR PDB; 2HPH; X-ray; 1.33 A; A=24-332.
DR PDB; 2IPL; X-ray; 1.20 A; A=24-332.
DR PDB; 2IPM; X-ray; 1.12 A; A=24-332.
DR PDB; 2IPN; X-ray; 1.15 A; A=24-332.
DR PDB; 2QW1; X-ray; 1.70 A; A=24-332.
DR PDBsum; 1GLG; -.
DR PDBsum; 2FVY; -.
DR PDBsum; 2FW0; -.
DR PDBsum; 2GBP; -.
DR PDBsum; 2HPH; -.
DR PDBsum; 2IPL; -.
DR PDBsum; 2IPM; -.
DR PDBsum; 2IPN; -.
DR PDBsum; 2QW1; -.
DR AlphaFoldDB; P0AEE5; -.
DR BMRB; P0AEE5; -.
DR SMR; P0AEE5; -.
DR BioGRID; 4259172; 16.
DR BioGRID; 853285; 1.
DR ComplexPortal; CPX-4341; Beta-methyl-D-galactoside/galactose ABC transporter complex.
DR DIP; DIP-35953N; -.
DR IntAct; P0AEE5; 8.
DR STRING; 511145.b2150; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR TCDB; 3.A.1.2.3; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AEE5; -.
DR jPOST; P0AEE5; -.
DR PaxDb; P0AEE5; -.
DR PRIDE; P0AEE5; -.
DR EnsemblBacteria; AAC75211; AAC75211; b2150.
DR EnsemblBacteria; BAE76627; BAE76627; BAE76627.
DR GeneID; 66673954; -.
DR GeneID; 949041; -.
DR KEGG; ecj:JW2137; -.
DR KEGG; eco:b2150; -.
DR PATRIC; fig|1411691.4.peg.91; -.
DR EchoBASE; EB0588; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_037628_3_1_6; -.
DR InParanoid; P0AEE5; -.
DR OMA; MWDAAMA; -.
DR PhylomeDB; P0AEE5; -.
DR BioCyc; EcoCyc:MGLB-MON; -.
DR BioCyc; MetaCyc:MGLB-MON; -.
DR EvolutionaryTrace; P0AEE5; -.
DR PRO; PR:P0AEE5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0015757; P:galactose transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015765; P:methylgalactoside transport; IMP:EcoCyc.
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; Direct protein sequencing;
KW Metal-binding; Periplasm; Reference proteome; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7012152,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 24..332
FT /note="D-galactose-binding periplasmic protein"
FT /id="PRO_0000031722"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:3057628,
FT ECO:0000269|PubMed:3600760, ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
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:0000269|PubMed:3057628,
FT ECO:0007744|PDB:2GBP"
FT SITE 97
FT /note="Interacts with membrane-bound trg signal transducer"
FT MUTAGEN 97
FT /note="G->D: Improductive interaction with trg."
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2FVY"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2IPM"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:2FVY"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2FVY"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2FVY"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:2FVY"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:2FVY"
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
