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Database: UniProt
Entry: V4R0N9_9CAUL
LinkDB: V4R0N9_9CAUL
Original site: V4R0N9_9CAUL 
ID   V4R0N9_9CAUL            Unreviewed;       798 AA.
AC   V4R0N9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=ABENE_19310 {ECO:0000313|EMBL:ESQ84968.1};
OS   Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ84968.1, ECO:0000313|Proteomes:UP000017837};
RN   [1] {ECO:0000313|EMBL:ESQ84968.1, ECO:0000313|Proteomes:UP000017837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ84968.1,
RC   ECO:0000313|Proteomes:UP000017837};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:ESQ84968.1}.
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DR   EMBL; AWGB01000062; ESQ84968.1; -; Genomic_DNA.
DR   RefSeq; WP_018083627.1; NZ_AWGB01000062.1.
DR   AlphaFoldDB; V4R0N9; -.
DR   STRING; 1121022.GCA_000376105_03943; -.
DR   PATRIC; fig|1121022.4.peg.3957; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000017837; 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; 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   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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..798
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004726340"
FT   DOMAIN          718..787
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   798 AA;  86494 MW;  997D310FF02954B7 CRC64;
     MKLKTPVLTR RLFGASTLAL SAVAGTAMAA KAKKETLPYK DASLTIDARV ADLLGRMTLE
     EKVAQLLCVW QKKGDIQDAT GKFDPAKASK VYPNGLGMVA RPSDQQGLAT TTGAGDSGAM
     GNRNAFNTAS HVNAMQKWAI EETRLGIPMI MHEEGLHGYV AKDATSFPQA IGLASSFDPP
     MATKIFSVAA REMRARGANF ALAPVVDVAR EPRWGRIEET YGEDPYLCGE MGKAAVIGFQ
     GETLPLAKDK VFATLKHMTG HGQPENGTNV GPAEVSERTL REDFFPPFEK IVKETQIRAV
     MPSYNEIDGV PSHANKWLLT TILRDEWGFK GVTVSDYFAI NEMISRHKLV PNVTEAAFRA
     FKAGVDIETP DNQTYGQLIE LVKAGRISED EINAVVHRIL EMKFQSGLFE NPYVDAKKAD
     ALTATPDAVA LAHEAATKSV VLLKNNGVLP LDAKKVGKLL VLGTHAKDTP IGGYSDVPRH
     VVSILEGVTA EGKKAGFEVA YSEGVRITEQ RIWGQDAINF TPDSVNDKLI ADAVEAAKSA
     DTILLVLGDN EQTSREAWAD NHLGDRDSLD LMGRQNDLAA AIFALKKPTV VFLLNGRPLS
     VNLLNEKADA LVEGWYMGQE TGWAAADILF GRANPGGKLP VSIARGVGQL PVFYNHKPTA
     RRGYLDGETS PLFPFGYGLS YTTFDISAPK LAKASIATTE TVTVSIDVAN TGKVKGDEVV
     QLYIRDDISS VTRPVKELKR FKRITLNPGE RQTVSFDITP ADLQFYNMDM QRVVEPGTFT
     ISAGPNSVDL KTATLTVI
//
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