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Database: UniProt
Entry: B2IMQ0_STRPS
LinkDB: B2IMQ0_STRPS
Original site: B2IMQ0_STRPS 
ID   B2IMQ0_STRPS            Unreviewed;       471 AA.
AC   B2IMQ0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ACB89796.1};
GN   OrderedLocusNames=SPCG_0544 {ECO:0000313|EMBL:ACB89796.1};
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89796.1, ECO:0000313|Proteomes:UP000001682};
RN   [1] {ECO:0000313|EMBL:ACB89796.1, ECO:0000313|Proteomes:UP000001682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89796.1,
RC   ECO:0000313|Proteomes:UP000001682};
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP001033; ACB89796.1; -; Genomic_DNA.
DR   RefSeq; WP_000151860.1; NC_010582.1.
DR   AlphaFoldDB; B2IMQ0; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GeneID; 66805740; -.
DR   KEGG; spw:SPCG_0544; -.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   Proteomes; UP000001682; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF122; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        364
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   471 AA;  54435 MW;  5DD2468225138A86 CRC64;
     MTIFPDDFLW GGAVAANQVE GAYNEDGKGL SVQDVLPKGG LGEATENPTE DNLKLLGIDF
     YHKYKEDITL FSEMGFNVFR TSIAWSRIFP KGDEEEPNEA GLKYYDELFD ELHAHGIEPL
     VTLSHYETPL YLARKYHGWI DRRMIHFYEK FARTVLERYK DKVKYWLTFN EVNSVLELPF
     TSGGIDIPKE NLSKQELYQA IHHELVASSL VTKIAREINS EFKVGCMVLA MPAYPMTPNP
     KDVWATHEYE NLNYLFSDVH VRGYYPNYAK RYFKEHDINI EFAAEDAELL KNYTVDFLSF
     SYYMSVTQSA LPTQYNSGEG NIIGGLVNPY LESSEWGWQI DPIGLRIILN RYYDRYQIPL
     FIVENGLGAK DQLIKDEFNN LTVQDDYRIQ YMKEHLLQVA EALQDGVEIM GYTSWGCIDC
     VSMSTAQLSK RYGLIYVDRN DDGNGTFNRY KKMSFTWYKG VIESNGESLF K
//
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