ID A0A5R9DWZ2_9LACT Unreviewed; 917 AA.
AC A0A5R9DWZ2;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=FEZ33_10445 {ECO:0000313|EMBL:TLQ39715.1};
OS Ruoffia tabacinasalis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ruoffia.
OX NCBI_TaxID=87458 {ECO:0000313|EMBL:TLQ39715.1, ECO:0000313|Proteomes:UP000306420};
RN [1] {ECO:0000313|EMBL:TLQ39715.1, ECO:0000313|Proteomes:UP000306420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAM 24227 {ECO:0000313|EMBL:TLQ39715.1,
RC ECO:0000313|Proteomes:UP000306420};
RA Roder T., Wuthrich D., Sattari Z., Von Ah U., Bar C., Ronchi F.,
RA Macpherson A.J., Ganal-Vonarburg S.C., Bruggmann R., Vergeres G.;
RT "The metagenome of a microbial culture collection derived from dairy
RT environment covers the genomic content of the human microbiome.";
RL Submitted (MAY-2019) 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 -!- 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:TLQ39715.1}.
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DR EMBL; VBSP01000051; TLQ39715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9DWZ2; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000306420; 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 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:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:TLQ39715.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..917
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038446495"
FT DOMAIN 243..553
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 803..903
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT REGION 35..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 100528 MW; 119FCD89DC63A9AA CRC64;
MKPKSWKERV LLCGLVLASV SSASMNTVVS ATSLGSGISQ SSQSSKVKIL AQADPYATED
NEADDPYAND DPYANDDPYA NDDDPYANDD PYANDDPYAN DDPYANDDPY ANDDPYANES
GDAADDPYAE ESEESEASAT TYDFEYTEFD DGVTKFGIVE NPNGGPKIGF SLSSGIQILT
EEVDGETYYF KDMNGNGKLD VWEDWREDTE TRAAALAEEL TTEQIAGLML FSSHQREQSE
GLTEDQIAFL ENDGVRNVLH AGPNDVEATV KWANEMQAFV ENLDNGLPII PVNFSSDPRS
GAGDTTGAYN AAGEDISRWP SNLGLAATFN PETMQQFSVM SSAEYRAMGL TTALGPQIEL
ATEPRWLRID GTFGEDIDLA SDMAEAYANQ SQSTYDEEGN DQGWGEDSIN IMIKHFPGDG
PGESGRESHT FEGKFGVYPG GNFDEHYQLF IDSGLNLSGE TAQVSAMMTS YSIQLDADGN
PLFGEDPVGT AYNEELISKL RDEEGFDGVL VTDWGVTRYN DENPDRPGGS AFGYEDATEA
ERHFHIIKAG LDMFGGNNAM QPILDAYELW EEAYDNGEVD QTADERFKES GKRIVRNTLL
VGAFENPYLV PEESAVTVAS EDKVEAGYQA QLDSIVMLKN KDNVIAEQDI ETFKDKVVYI
PMTSNVSLPL TEESTTTHKS TLNIESAEQY FKEVVTDTAT TDEEGNITEF ERVTDLSNVD
LVIVGMESPN NGSNFSNAGI NADNEYYPLS LQYRPYTADG DNVREVSIGG DTLEDGTKEN
RSYKGNTSII GNEADLDAVL EAVELVEASG RDIPIIVVMK AKNPVIMSEF EELVDAIVVG
FGVDDSAYLE VILGNHEPQG LLPIQFPANM DTVESQQEDV ARDMEPYVDS EGNTYDFGYG
INYSGVIQDE RTEKYVD
//
