ID G2ZB21_LISIP Unreviewed; 722 AA.
AC G2ZB21;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=LIV_1705 {ECO:0000313|EMBL:CBW86192.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW86192.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW86192.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR687253; CBW86192.1; -; Genomic_DNA.
DR RefSeq; WP_014093088.1; NZ_CVPH01000006.1.
DR AlphaFoldDB; G2ZB21; -.
DR GeneID; 57076710; -.
DR KEGG; liv:LIV_1705; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_9; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000001286; Chromosome.
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:SF121; PERIPLASMIC 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 640..709
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 722 AA; 79359 MW; 86B117021E013744 CRC64;
MKQENLTALL TEMTLDEKIA QCLQLSPFLF KGAKKNAELT GPVLQEMKLT DAHTENAGSV
LGSSSAEDML GIQETYLKTN RLGIPLIFMA DVIHGYKTVF PIPLALGCSF DRETVRTMAE
VAALEATADG HHVTFSPMLD LVRDPRWGRV MESTGEDPFL NSELGKAMVA GYQGDASKLH
ENKANLAACV KHFAAYGAAE AGLEYNTVNM STRELYQNYL PAYEAAIHAG AKLVMTAFNV
VDGVPATMNK WLNRDVLRQG MNFDGVLISD WGAVAEVINH GTARNPAEAA QFSMEAGVDM
EMMTTCYIHE LKGLIEANKL SESLVDEAVS RILQLKNDLG LFEDPYRGLK GKSRQTDILT
PENRRKSREA GLESAVLLEN KQQILPLAET TKIALIGPLA TSNDILGGWN VYGDEKDGIN
VETGLLEVFS ELTTVSTDYT TLTAENKAEI EKAIQSAEVV VLALGEKNEW GGEAGSLATI
RLPESQYDLA KYAQSFGKPV VITLFNGRPL EVKELAEASD ALLELWFPGT EAGRVTADLL
VGKSNPSGKL SMSFPQTTGQ IPVYYNHLRT GRPQTEANKG ERYVSHYLDI PNEPYYPFGY
GKSYSEFEWK TAELPKQIQL GEPLEVKVTL KNKSGIAGKE VIQIYLQDVT ATISRPVKEL
KAFEKVALQP GEEKTVAFEL TSEAFSFYNH QLEKVQEPGL HRIFVGTSSE EVDTFELEVG
EV
//
