ID A0A101ST56_9ACTN Unreviewed; 1000 AA.
AC A0A101ST56;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AQJ64_27945 {ECO:0000313|EMBL:KUN79577.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN79577.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN79577.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN79577.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) 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:KUN79577.1}.
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DR EMBL; LMWW01000047; KUN79577.1; -; Genomic_DNA.
DR RefSeq; WP_055633963.1; NZ_LIQS01000164.1.
DR AlphaFoldDB; A0A101ST56; -.
DR STRING; 1943.AQJ64_27945; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000052982; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
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 InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR005087; CBM_fam11.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF03425; CBM_11; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00237; Calx_beta; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1000
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007106538"
FT DOMAIN 202..307
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
SQ SEQUENCE 1000 AA; 105930 MW; 8D9CB2AE5EE9B0C1 CRC64;
MPRTALLVST ALFAALLSPT AVRAAADPAP TPVDRFEGEV PFASQPAEGI FTWGSDADDP
PALRLADRAD APEGERVLTG DYDISGWGGF THDYAATGPA HDWSAHQGIR FWWQGHGDGR
RIAFEIKDGG AHGEASELWT TSFTDDFTGW KRIEIPFADF RYRTDYQPVG GIDHVLGLTQ
MWGYAVTLPT GAGGDFAMDG VELYGRADQS LRASVTTDAA VYPVAEGGAA TVRVTLATTG
AAPVDEPVTV TYGTADGTAE PGRDYTPVTG TLTFPAGTPS GTSRTVRIPT LRDRAAEAAE
TIPLTLTVTG AKAPAETPQV VIDAHGLPYL NSKLPVKRRV ADLLSRMSLA EKAGQMTQAE
RGALTAPGDI AAYDLGSLLS GGGSTPTPNT PEAWAKMIDA FQLRTRATRF QIPLIYGVDA
VHGHNNLVGA TVMPHNIGIG ATRDPQLAHR TGEVTAAEVR ATGVPWDFAP CLCVTRDERW
GRSYESFGED PALVESMETV IQGLQGAPDG RDLKDDDKVL ATAKHFVGDG GTTYGSSTTG
SYTIDQGVTE VTRKQLEAVH LAPYREAVDR GVGTVMPSYS SLDIAGDGQG PVKMHARADM
INGVLKGRMG FDGFVISDWA AIDQLPGDYA SDVRTSVNAG LDMIMVPYAY QDFTRTLTDE
VTAGRIAERR IDDAVSRILT QKIRLGLFER PYADTSGAAD IGSAAHRAVA RRAAAESQVL
LKNSGGLLPL KKTQKVYVAG SNADDIGNQT GGWTVTWQGA SGNTTPGTTI LEGIRRTGAP
VTYSKDASAP LTGYDVGVVV VGETPYAEGV GDVGNGNDLE LSPADRAAVD RVCAAMKCAV
LIVSGRPQLI GDRLGPIDAL VASWLPGTEG DGVADVLYGR RPFTGRLPVT WPRSEAQLPI
NVGDPVYDPQ YPYGWGLTTL TKTPGGGLAA LYRLADAAGR AHTAQAGRSA VEQARRIVER
RIADRITAAS AKPFAEADHL LLTGRYARAV RKLIEAYRAG
//
