ID   Q8E617_STRA3            Unreviewed;       475 AA.
AC   Q8E617;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=6-phospho-beta-glucosidase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=gbs0811 {ECO:0000313|EMBL:CAD46455.1};
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110 {ECO:0000313|EMBL:CAD46455.1};
RN   [1] {ECO:0000313|EMBL:CAD46455.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316 {ECO:0000313|EMBL:CAD46455.1};
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; AL766847; CAD46455.1; -; Genomic_DNA.
DR   RefSeq; WP_000215675.1; NC_004368.1.
DR   AlphaFoldDB; Q8E617; -.
DR   KEGG; san:gbs0811; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   Proteomes; UP000000823; 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   475 AA;  54438 MW;  14927AB2A661F6F0 CRC64;
     MTVFPKHFLW GGAVAANQVE GAFRTDGKGL SVQDVLPNGG LGDFTAKPTP DNLKLEAIDF
     YHNYKNDIKL FAEMGFKVFR TSIAWSRIFP NGDDSAPNEA GLQFYDNLFD ELLKYNIEPL
     VTLSHYETPL HLAKTYNGWA DRRLIAFFEK FAQTVMERYK DKVKYWLTFN EVNSILHMPF
     TSGAIMTDKS QLSPQELYQA IHHELVASAR VTKLGRSINP NFKIGCMILA MPAYPMTSDP
     RDVLAARQFE QHNLLFSDIH VRGKYPTYIQ SYFKNNGIKI KFEEGDEEVL AQNTVDFLSF
     SYYMSVTQAY DFENYQSGQG NILGGLTNPH LTTSEWGWQI DPIGLRLVLN QYYERYQIPL
     FIVENGLGAK DQLIETLDGD YTVEDDYRID YMNQHLVQVA KAIEDGVEIM GYTSWGCIDC
     VSMSTAQLSK RYGLIYVDRN DDGTGSLQRY KKKSFGWYQK VIKTNGQSLF EHHNR
//