(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 129.
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]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
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]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=8132630;
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}.
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   SMR; P23905; -.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   PaxDb; P23905; -.
DR   PRIDE; P23905; -.
DR   EnsemblBacteria; AAL21094; AAL21094; STM2190.
DR   GeneID; 1253712; -.
DR   KEGG; stm:STM2190; -.
DR   PATRIC; fig|99287.12.peg.2317; -.
DR   eggNOG; ENOG4105EMA; Bacteria.
DR   eggNOG; COG1879; LUCA.
DR   HOGENOM; HOG000212345; -.
DR   KO; K10540; -.
DR   OMA; MWDAAMA; -.
DR   PhylomeDB; P23905; -.
DR   BioCyc; SENT99287:STM2190-MONOMER; -.
DR   EvolutionaryTrace; P23905; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; 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   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;
DR   PRODOM; P23905.
DR   SWISS-2DPAGE; P23905.
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   CA_BIND         157..165
FT                   /note="First part of site"
FT   CA_BIND         227..228
FT                   /note="Second part of site"
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:0000244|PDB:1GCA"
FT   HELIX           38..52
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          57..63
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           68..80
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          84..88
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           93..95
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           96..105
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          110..115
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           119..123
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          128..132
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           135..152
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           154..156
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          161..170
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           176..191
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          196..203
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           208..219
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           224..226
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          229..234
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           235..247
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           262..269
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          275..278
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           281..296
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   TURN            301..304
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          313..315
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   STRAND          319..321
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   TURN            323..325
FT                   /evidence="ECO:0000244|PDB:1GCA"
FT   HELIX           326..328
FT                   /evidence="ECO:0000244|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
//

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