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Database: UniProt
Entry: V4P7Y1_9CAUL
LinkDB: V4P7Y1_9CAUL
Original site: V4P7Y1_9CAUL 
ID   V4P7Y1_9CAUL            Unreviewed;       756 AA.
AC   V4P7Y1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=AEAC466_10465 {ECO:0000313|EMBL:ESQ84161.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ84161.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ84161.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ84161.1,
RC   ECO:0000313|Proteomes:UP000017826};
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:ESQ84161.1}.
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DR   EMBL; AWGE01000008; ESQ84161.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4P7Y1; -.
DR   STRING; 1282362.AEAC466_10465; -.
DR   PATRIC; fig|1282362.3.peg.2069; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000017826; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51318; TAT; 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:UP000017826};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..756
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004724588"
FT   DOMAIN          675..744
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   756 AA;  80379 MW;  9FD1C9E99892C174 CRC64;
     MNAFNPSRRF FLKGAVATAA LVPVAAPGFA KVTPAPDPFI EKLIKSLTVE EKAGQLSLYG
     DSTRFDGPPI NPTSEQAQTK DKVKADIAAG KITGLFNGIG VAGGRELQQV AVEQSRSKIP
     LIFGGDIIHG LKTTFPIPLG ESASFDTDLA MRTARASALE ATAKGIHWTF APMVDVARDQ
     RWGRVAEGAG EDTWLGIQLA VARVKGFQGN SLKDDRTMLA CPKHFAAYGA VQGGMEYNTV
     DIPETTLREV HLPPFKAAFD AGAITTMSSF NDIAGVPSTG NHYLLTDILR GEWGFKGLVV
     SDYTSEEELI LHGYAADGAD ATAKSLNAGC DMSMQSGLYI KYLPELVKSG KVKMATLDEA
     VRRVLYVKKA LGLFDNPYRS LDLGREQTDV RHADTIALAR EAGRKSCVLL KNEGNLLPLP
     KTGKTVALIG PFGNDKENCP GPWAVFPDIA SCVPLEPAFR AVLGDRLTVV KGSDVEAPID
     GGLALAVKAA QAADIVVLAI GEAGNMSGEA QSRVDISVPV PQLALAEAVA ATGKPVVVLL
     KHGRAIALTG AVRNAQAILC TWFLGSEEGH SVADLVFGDF APQGRLPVSF PQASGQEPYY
     YNHRITGRPQ ISDDKNFKAR YREVTNEALY PFGHGLTYST LSYGATAVSA ATLTLTGSIQ
     VTATVTNTGA RRAHEVAQLY IHDKVASMTQ PIRALKGIKH LDLEPGQSAT VTFELTAADL
     AFVHPNLKTT AEPGRFDVWV APSATGGTPA TFELKA
//
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