ID   I9PLV0_9BACE            Unreviewed;       769 AA.
AC   I9PLV0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF1061_03539 {ECO:0000313|EMBL:EIY17451.1};
OS   Bacteroides caccae CL03T12C61.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997873 {ECO:0000313|EMBL:EIY17451.1, ECO:0000313|Proteomes:UP000002965};
RN   [1] {ECO:0000313|EMBL:EIY17451.1, ECO:0000313|Proteomes:UP000002965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL03T12C61 {ECO:0000313|EMBL:EIY17451.1,
RC   ECO:0000313|Proteomes:UP000002965};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides caccae CL03T12C61.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIY17451.1}.
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DR   EMBL; AGXF01000018; EIY17451.1; -; Genomic_DNA.
DR   RefSeq; WP_005682249.1; NZ_JH724080.1.
DR   AlphaFoldDB; I9PLV0; -.
DR   GeneID; 75112556; -.
DR   PATRIC; fig|997873.3.peg.3683; -.
DR   HOGENOM; CLU_004542_5_1_10; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000002965; Unassembled WGS sequence.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..769
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003723384"
FT   DOMAIN          689..758
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   769 AA;  84724 MW;  A544795AB3631D37 CRC64;
     MIYKKLSLLI LFFATGLLTA SAQKSPQDMD RFIDALMKKM TTEEKIGQLN LPVTGEITTG
     QAKSSDIAGK IKKGEVGGLF NLKGVEKIRE VQKQAVEESR LGIPLLFGMD VIHGYETMFP
     IPLGLSCTWD MAAIEESARI AAVEASADGI SWTFSPMVDI SRDPRWGRVS EGNGEDPFLG
     AMIAEAMVRG YQGKDMKRND EIMACVKHFA LYGASEAGRD YNTVDMSRQR MFNDYMLPYE
     AAVEAGVGSV MASFNEVDGI PATANKWLMT DILRGQWGFN GFVVTDYTGI SEMIDHGIGN
     LQTVTARAIN AGVDMDMVSE GFVGTLKKSI QEGKVSMETL NTACRRILVA KYKLGLFDNP
     YKYCDPKRPA RDIFTKAHRD AARRIAAESF VLLKNDSPDG NPNGNPLLPF NPKGNIAVIG
     PLANSRANMP GTWSVAAVLD RCPSLVEGLK EMTAGKANIM YAKGSNLISD AAYEERATMF
     GRSLNRDNRT DQQLLDEALN VARRSDIIIA ALGESSEMSG ESSSRTNLDL PDVQQNLLKE
     LLKTGKPVVL VLFTGRPLTL NWEQEHVPAI LNVWFGGSEA AYAIGDALFG YVNPGGKLTM
     TFPKNVGQIP LYYAHKNTGR PLGQGKWFEK FRSNYLDVDN EPLYPFGYGL SYTTFSYSDI
     DLSHSSMDMN GSLTAAVTVT NTGTWPGSEV VQLYIRDVVG SSTRPVKELK GFQKIFLEPG
     EMKIVRFKIA PEMLRYYNYD LQLVAEPGDF EVMIGTNSRD VKTARFTLN
//