ID A0A0B5DQA1_9ACTN Unreviewed; 1008 AA.
AC A0A0B5DQA1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BJY54_004613 {ECO:0000313|EMBL:MBB4794001.1}, CP978_23795
GN {ECO:0000313|EMBL:QEV41175.1}, SNOD_23470
GN {ECO:0000313|EMBL:AJE42671.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE42671.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE42671.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE42671.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV41175.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV41175.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4794001.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4794001.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP009313; AJE42671.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4794001.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV41175.1; -; Genomic_DNA.
DR RefSeq; WP_043444104.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_23470; -.
DR KEGG; snq:CP978_23795; -.
DR HOGENOM; CLU_006721_0_0_11; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; 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, ECO:0000313|EMBL:MBB4794001.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1008
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041036852"
FT DOMAIN 205..310
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
SQ SEQUENCE 1008 AA; 105867 MW; 380C3813142EAA06 CRC64;
MRRTALLASA ALLATLLPLG AAGVASGAGD PAPVPIDRFE GEVPFASQPA EGIFTWGGDA
DDPPTLQLTG RADAPEGDKV LTGTYDISGY GGFTHDFAAD RPAHDWSAHQ GIRFWWEGRD
NGKKIAFEIK DGGAHGEASE LWTTSFTDDF TGWKQIEIPF ADFTYRTDYQ PVGGIDHVLG
LTQMWGYAVT LPTGVKGGFA MDDVELYGRA DQSQRAFVTT DSAVYPVTEG GTAQVKVSVA
TTGSAPLDEP VTVGYETAGG SAGSGSDYTP VKGTLVFPAG TASGSTRTIK VATLKDKAAE
PAETIPLKLT VTGAKAPEET PQVVIDAHGL PYLDSKLSVR KRVADLLSRM SLEEKAGQMT
QAERSAVASG GDIAAYALGS LLSGGGSTPT PNTPEAWAKM IDSFQLRAQA TRFQIPLIYG
VDAVHGHNNL AGATVMPHNI GIGATRNPQL AEETGAVTAI EVRATGVPWD FAPCLCVTRD
ERWGRSYESF GEDPALVRSM ETVIQGLQGR ADGRDLSRND KVLGTAKHFV GDGGTAYGSS
TTGSYTTDQG VTKVTRQELE AVHLAPYQTA VDRGIGSVMP SYSSLDIIGD GQGPVKMHAR
ADMLNGVLKD RMGFEGFVIS DWAAIDQLPG GTAAQVRASI NAGLDMIMVP YEYQGFRTTL
IDEVKAGRIS QKRIDDAVSR ILTQKFKLGL FERPYTDTRN ASKIGSTAHR AVARQAAAES
QVLLKNAHDL LPLTKKQKVY VAGSNADDLG NQTGGWTITW QGESGTHTQG TTILQGMRKA
APGATITYSK DASAPVSGYD VGVVVVGETP YAEGVGDVGN GHDLQLSAAD KAAVDKVCGA
MKCAVLIVSG RPQLVGDRLG AVDALVASWL PGTEGDGVAD VLYGKRPFTG QLPVTWPKSE
AQLPINVGDA SYDPQFPYGW GLTTLTPVPK GGTATLKVLG LAAAVAEKTG SARTGREIVT
QARLLVQQKI GSGITASVSG PFADADHLLL TGKYAAAVAK LTEAYKAA
//
