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Database: UniProt
Entry: U5SA66_9LACT
LinkDB: U5SA66_9LACT
Original site: U5SA66_9LACT 
ID   U5SA66_9LACT            Unreviewed;       721 AA.
AC   U5SA66;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=Q783_07945 {ECO:0000313|EMBL:AGY82120.1};
OS   Carnobacterium inhibens subsp. gilichinskyi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY82120.1, ECO:0000313|Proteomes:UP000017469};
RN   [1] {ECO:0000313|EMBL:AGY82120.1, ECO:0000313|Proteomes:UP000017469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN1359 {ECO:0000313|EMBL:AGY82120.1,
RC   ECO:0000313|Proteomes:UP000017469};
RX   PubMed=24285647;
RA   Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT   "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT   (DSM 27470T).";
RL   Genome Announc. 1:e00985-13(2013).
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};
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DR   EMBL; CP006812; AGY82120.1; -; Genomic_DNA.
DR   RefSeq; WP_023178674.1; NC_022606.1.
DR   AlphaFoldDB; U5SA66; -.
DR   STRING; 1266845.Q783_07945; -.
DR   KEGG; caw:Q783_07945; -.
DR   PATRIC; fig|1266845.5.peg.1482; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_9; -.
DR   Proteomes; UP000017469; 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, ECO:0000313|EMBL:AGY82120.1}.
FT   DOMAIN          638..707
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   721 AA;  80089 MW;  A3DC0FF91E29381D CRC64;
     MDTTQLKHLL GEMTRAEKIG QMVQLAGEFY KEEDSENTGP MHEMNMTPKK MTVSGSVLGI
     SGAETLINIQ KEHLAKSRLG IPLLFMADVV HGYRTIFPVP LAMASTWQPE LVEESANVSA
     TEAAVSGLHV TFAPMVDLVR DARWGRVMES TGEDPYLNQL YARAFVRGYQ GQDLKNDPFS
     VAACVKHFAG YGAPVAGREY NTVELSERTL KEMYLPAYQA GISEGSKLVM TAFNSLEGVP
     ATANKPLMRE TLRKELGFEG VLISDWASVG ELIPHGIAKD LKQAGELAIQ AGVDIEMMTG
     GYLNYLNELI DEGKVSEELL NEAVWRILTL KNELGLFENP YRGANSELEN NLVFSKEHRE
     KARIVAEESI VLLKNEKQVL PLTHHQKVAL IVPKDQSKDV LGPWSWKGEP SESVSVYEGL
     LNHISKEAIV VKTIDHSKND RPKDWLDDVS TADVIVAALG ESSYMSGEGA SRSNIKLPAE
     QIQVIKELRT LNKPIVLILF NGRPLDLTDV VQDVDSILGA WFPGTEAGTA IGNILYGTKN
     PSGKLTMSFP RAVGQVPLYY NQDNTGRPLT AYNQEDKYLS RYLDVDNRPL FPFGYGLSYT
     QFSYSPMKVT LSKSEREQTD KIIVETTITN SGKVTGSEVV QLYIRDKVGQ VVRPIKELKR
     FKKILLEPGE VATILFELNQ QDLEYVHQDL SVSVESGEFD LMIGSNSEEV ETTTVYLELK
     K
//
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