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Database: UniProt
Entry: B0T4K9_CAUSK
LinkDB: B0T4K9_CAUSK
Original site: B0T4K9_CAUSK 
ID   B0T4K9_CAUSK            Unreviewed;       808 AA.
AC   B0T4K9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE   Flags: Precursor;
GN   OrderedLocusNames=Caul_1832 {ECO:0000313|EMBL:ABZ70961.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ70961.1};
RN   [1] {ECO:0000313|EMBL:ABZ70961.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ70961.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000927; ABZ70961.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0T4K9; -.
DR   STRING; 366602.Caul_1832; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; cak:Caul_1832; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_5; -.
DR   OrthoDB; 9781691at2; -.
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: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.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABZ70961.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..808
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002753350"
FT   DOMAIN          727..796
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          85..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  87625 MW;  1B0940EDBA78A8BF CRC64;
     MSSQTAVTRR TLGVSLAALA AASSTLARAA APPKAGKVER ALYKDPTQSI ELRVRDLLSR
     MTLEEKAAQL VGIWLTKAKI QTPNGDFSPE EASKNFPDGL GQISRPTDRR GLKPATVVGA
     AAGAEDGSIG RNAKETARYI NAAQKWAMEK TRLGVPMLMH DEALHGYVAR DATSFPQAIA
     LASTFDTEMT EKVFAVAARE MRARGSNIAL APVVDVARDP RWGRIEETYG EDPHLCAEIG
     LAAIRGFQGK TLPLAPDKVF VTLKHMTGHG QPENGTNVGP AQIAERTLRE NFFPPFERAV
     KELPVRSVMP SYNEIDGVPS HANRWLLTDI LRKEWGYKGS VQSDYFAIKE LMGRHKLTDD
     LGETAVMAMN AGVDVELPDG EAYALLPQLV KVGRIPQAAV DQAVERVLTM KFEGGLFENP
     YADEKTADAK TATPDAIALA REAARKAVVL LKNDKGVLPL NPSKFKRLAL LGTHAKDTPI
     GGYSDTPRHV VSIYEGLQAE AKKSGFTLDY AEAVRITEAR IWAQDEVKLV DPAVNAKLIA
     EAVEVAKQAD VIVMVLGDNE QTSREAWADN HLGDRDSLDL IGQQNDLARA IFDLGKPTVV
     FLLNGRPLSI NLLAQRADAV IEGWYLGQET GNAAADILFG RANPGGKLPV SIARDVGQLP
     IYYNRKPTAR RGYLLGDTSP LYPFGFGLSY TTFDISAPRP AKAEIGANES VKVEIDVINT
     GKVAGDEVVQ LYIHDEAASV TRPVLELKHF KRVTLAPGAK QTVTFEVSPL DLSLWNLEMK
     RVVEPGKFTL LSGPNSAQLK PATLTVMA
//
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