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DGAL_HAEIN
ID   DGAL_HAEIN              Reviewed;         331 AA.
AC   P44883;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=HI_0822;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-29.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
CC   -!- FUNCTION: This protein is involved in the active transport of galactose
CC       and glucose. {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-229. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22481.1; ALT_INIT; Genomic_DNA.
DR   PIR; G64096; G64096.
DR   RefSeq; NP_438982.2; NC_000907.1.
DR   RefSeq; WP_010869062.1; NC_000907.1.
DR   AlphaFoldDB; P44883; -.
DR   SMR; P44883; -.
DR   STRING; 71421.HI_0822; -.
DR   EnsemblBacteria; AAC22481; AAC22481; HI_0822.
DR   KEGG; hin:HI_0822; -.
DR   PATRIC; fig|71421.8.peg.863; -.
DR   eggNOG; COG1879; Bacteria.
DR   HOGENOM; CLU_037628_3_1_6; -.
DR   PhylomeDB; P44883; -.
DR   BioCyc; HINF71421:G1GJ1-863-MON; -.
DR   Proteomes; UP000000579; 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   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   Calcium; Direct protein sequencing; Metal-binding; Periplasm;
KW   Reference proteome; Signal; Sugar transport; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:10675023"
FT   CHAIN           25..331
FT                   /note="D-galactose-binding periplasmic protein"
FT                   /id="PRO_0000031724"
FT   BINDING         38
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         38
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT   BINDING         115
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         115
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         160
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         162
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         176
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         176
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT   BINDING         178
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         178
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT   BINDING         182
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         182
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEE5"
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         235
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000250|UniProtKB:P23905"
FT   BINDING         235
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"
SQ   SEQUENCE   331 AA;  35518 MW;  D4A0E639D9FD22A2 CRC64;
     MKKTAVLSTV AFAIALGSAS ASFAADNRIG VTIYKYDDNF MSLMRKEIDK EAKVVGGIKL
     LMNDSQNAQS IQNDQVDILL SKGVKALAIN LVDPAAAPTI IGKAKSDNIP VVFFNKDPGA
     KAIGSYEQAY YVGTDPKESG LIQGDLIAKQ WKANPALDLN KDGKIQFVLL KGEPGHPDAE
     VRTKYVIEEL NAKGIQTEQL FIDTGMWDAA MAKDKVDAWL SSSKANDIEV IISNNDGMAL
     GALEATKAHG KKLPIFGVDA LPEALQLISK GELAGTVLND SVNQGKAVVQ LSNNLAQGKS
     ATEGTKWELK DRVVRIPYVG VDKDNLGDFL K
 
 
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