ID   U2NJ47_9BACT            Unreviewed;       763 AA.
AC   U2NJ47;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF9135_1010 {ECO:0000313|EMBL:ERK38140.1};
OS   Segatella baroniae F0067.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK38140.1, ECO:0000313|Proteomes:UP000016648};
RN   [1] {ECO:0000313|EMBL:ERK38140.1, ECO:0000313|Proteomes:UP000016648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0067 {ECO:0000313|EMBL:ERK38140.1,
RC   ECO:0000313|Proteomes:UP000016648};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK38140.1}.
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DR   EMBL; AWEY01000044; ERK38140.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2NJ47; -.
DR   PATRIC; fig|1115809.3.peg.2492; -.
DR   Proteomes; UP000016648; 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   Reference proteome {ECO:0000313|Proteomes:UP000016648};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..763
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004633065"
FT   DOMAIN          681..750
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   763 AA;  83902 MW;  AFFC871CBB9A3589 CRC64;
     MTNCKKLWAA LAMGLALSPA VARQSGPTKM NSFIDNLMSR MTLQEKLGQL NLPVSGDIVT
     GQAKSSGVAE KIRRGAVGGL FNLKGVEQIR EMQKVAVEQS RLRIPLIFGM DVIHGYETVF
     PIPLAISCTW DMQAVENAAR VAAVEASADG ICWTFSPMVD ICRDPRWGRM AEGNGEDPFL
     GSAIARAMVK GYQGDDLSLK NTVMACVKHF ALYGGAEAGR DYNTVDMSRW RMFNEYFPPY
     EAAAKAGAGS FMTSFNVVDG IPATANRWLM TDVLRNRWGW DGFVVTDYTA ISEMTAHGMG
     DLQQVSALAL NAGTDMDMVA DGFIGTLEKS LKEGKVTMAS IDRACRRVLE AKYKLGLFDD
     PYRYLDKKRP AKDIYTPQHR ADARRVAAES FVLLKNDDLT LPLRRQGRIA LVGPLGDTPA
     NMPGTWSVAV AFDKCKSLFQ AMKDAVKDKA VVTYAKGSNI MDDKQMEANG SMFGREIRDD
     RTAEQMLEEA VGVAREADVI VAAVGETSEM SGECGSRSDL TLPEAQRRLL LALKATGKPV
     VLVNFSGRAT VMTWETEHFS TILNVWFGGS EAGDAICDVL FGDRVPSGKL TVTMPKSVGQ
     IPLYYNHFNT GRPLEPGKWF SKFRSNYLDI DNEPLFPFGY GLSYTTFKYA NLRLSADTMQ
     ADGTLTATVD VTNTGRCDAD EVVQLYIRDL VGSVVRPVKE LKGFERVHLK QGETRAVSFT
     IDASLLKFYD ANLDFVCEPG DFEVMVGPNS RDVETKRFTV EGL
//