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
//