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
//