ID W7D7D6_9LIST Unreviewed; 756 AA.
AC W7D7D6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=PRIP_08772 {ECO:0000313|EMBL:EUJ44917.1};
OS Listeria riparia FSL S10-1204.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265816 {ECO:0000313|EMBL:EUJ44917.1, ECO:0000313|Proteomes:UP000019248};
RN [1] {ECO:0000313|EMBL:EUJ44917.1, ECO:0000313|Proteomes:UP000019248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1204 {ECO:0000313|EMBL:EUJ44917.1,
RC ECO:0000313|Proteomes:UP000019248};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(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 -!- 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:EUJ44917.1}.
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DR EMBL; AODL01000009; EUJ44917.1; -; Genomic_DNA.
DR AlphaFoldDB; W7D7D6; -.
DR PATRIC; fig|1265816.5.peg.1736; -.
DR Proteomes; UP000019248; 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; 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:SF16; LYSOSOMAL 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 672..741
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 756 AA; 82721 MW; 81BA90BB1AC2F288 CRC64;
MMANYLDATC DVTERVADLL GRMTLVEKCG QLNQRLYGWD TFVRDGEDFD VTAVFKDEVT
TFGGIGALYG LFRADPWSGM NHENGISREN SARVANLLQR YVMENTRLGI PMLISEEVPH
GHQALDSESY PVNLARGASF NRELQREIAT AIATEIRDKG VHLALASALD IMRDPRWGRA
EECFSEDPYL AAEFTKSITT GFQESGEIAV ILKHFAAQGE PVGGHNSGPV SIGMRELREI
FLPPMVAATD ALGVMAAYNE IDGVPCHANA DLLTGILRDE LGFEGIVMAD GCALDRLLNL
MPDTKKAAAL GLTAGVDLSL WDSVYPDLAA AVTAGEVGEA LVDRAVSRVL RLKFELGLFE
KPYVTEKVAE RSASWRIWNL QAAREAICLL ENRKNVLPLR DAKHIAVIGP NADALYNQLG
DYTAPQNMTD GVTILQGLQN LAPENVTISY EKGSEVREKV INGVEKAVQL ANSADVIVLA
LGGSSARNFD MEFLNNGAVS SKGPNMDAGE NVDVADLALP DAQIELFQAV RALGKPVVVV
LVQGRPNAIP EISEQADALL TAWYPGAQGG TAVAEVLFGM TNPSGKLPVS IPRSSGQLPV
YYNQKVGEYK EDYFDERGSA LYNFGYGLSY SDFEYQKIET TRTNLTIAEL EAGEQFEFRI
TIANKSDVAG QEVVQLYIHD EEASITRRKK ELKDFQKIEI GARKTQEVIL KIGLAELQIW
SIKNRWELEA GNVRIFVGGG SDTTLETMIQ IKNEVV
//
