ID G2NFR8_STREK Unreviewed; 1028 AA.
AC G2NFR8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE Flags: Precursor;
GN ORFNames=SACTE_4739 {ECO:0000313|EMBL:AEN12565.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12565.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN12565.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN12565.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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}.
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DR EMBL; CP002993; AEN12565.1; -; Genomic_DNA.
DR RefSeq; WP_014048522.1; NC_015953.1.
DR AlphaFoldDB; G2NFR8; -.
DR STRING; 862751.SACTE_4739; -.
DR KEGG; ssx:SACTE_4739; -.
DR PATRIC; fig|862751.12.peg.4913; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_006721_0_0_11; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000001397; Chromosome.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1028
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039571239"
FT DOMAIN 48..233
FT /note="CBM11"
FT /evidence="ECO:0000259|Pfam:PF03425"
FT DOMAIN 256..306
FT /note="Calx-beta"
FT /evidence="ECO:0000259|Pfam:PF03160"
FT DOMAIN 374..703
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 742..941
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 1028 AA; 107532 MW; DFB8D615A5D3E1A4 CRC64;
MPRIPYTRAR HRARPVTAAL AAAAVLGSLL AGAVPSAAAD GDDPAPVLVD RFEGEVPFGG
PPADSLFTWG GDADDHPTLA FEERADAPEG DKVLAGTYDI SGYGGYSHEF AVGEPPADWT
AHQGIRFWWY GQNTAPLPPG SGKRVHFEIK DGGAHGGASE LWTTSFTDDW EGWHQVEIPF
ADFVYRADYQ PVGGIDQVLG LDEMWGYALT LPTGAPGSFA MDAVELYGKA DPALKASVVV
GSAVHPVKDG GTADIGISVA TTGSGPLEEP VTVAYTTRGG TAEPGTDYTP VSGTHTFPAG
TASGTTHTVS VATAEAEAPG AAKTIPLELT VTGAKPPKEN PQVVIDAHGL PYQDAKLPVE
KRVKDLLARM SPAEKAGQMT QAERNALSSQ GDIAAYDLGS LLSGGGSVPT PNTPEAWAKM
IDGYQLRAQA TRFQIPLIYG VDAVHGHNNV VGSTIMPHNI GIGAGRDPKL AERTGAVTAN
EVRATGVPWD FAPCVCVTRD ERWGRSYEAY GEDPALVEAM ETVITGMQGH ASGRDLARDD
KVLATAKHYV GDGGTEFGSS TTGSYTIDQG VTKVTRQELE AVHLAPFAES VKRGVGTVMP
SYSSLDVIGD GVGPVKMHAH AEMINGVLKD RMGFEGFVVS DWQAIDQIPG DYASDVRTSV
NAGLDMIMVP TAYQQFTRTL QDEVAAGRIG QARIDDAVSR ILTQKFRLGL FEKPYADPAH
LDEVGSPAHR AVAREAAAKS QVLLKNDGAL LPLKTSQKVY VAGSNADDLG NQAGGWTISW
QGASGATTQG TTILEGIRKT GAKPTYSKDA SAPTDGYDVG VVVVGETPYA EGIGDVGNGH
DLELGDADQK AVDTVCAAMR CAVLIVSGRP QLIGDRLGDI DALVASWLPG TEGDGVADVL
YGKRAFTGQL PVTWPKSESQ LPINVGDSAY DPQFPYGWGL TTLKKAPGGG ELTLAALAVA
AQVAQKAGLG STPAGKAIVD QARLMVQQKT GGKLTAKVSK PFAEADHLLL TGDLTGAVAE
LRTAYRAA
//
