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Database: UniProt
Entry: C6XLK5_HIRBI
LinkDB: C6XLK5_HIRBI
Original site: C6XLK5_HIRBI 
ID   C6XLK5_HIRBI            Unreviewed;       850 AA.
AC   C6XLK5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   OrderedLocusNames=Hbal_0209 {ECO:0000313|EMBL:ACT57911.1};
OS   Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hirschia.
OX   NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT57911.1, ECO:0000313|Proteomes:UP000002745};
RN   [1] {ECO:0000313|Proteomes:UP000002745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC   {ECO:0000313|Proteomes:UP000002745};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; CP001678; ACT57911.1; -; Genomic_DNA.
DR   RefSeq; WP_012778069.1; NC_012982.1.
DR   AlphaFoldDB; C6XLK5; -.
DR   STRING; 582402.Hbal_0209; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; hba:Hbal_0209; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_9_1_5; -.
DR   Proteomes; UP000002745; Chromosome.
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; 2.60.120.430; Galactose-binding lectin; 1.
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   InterPro; IPR041443; Exop_C.
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   PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF18559; Exop_C; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACT57911.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..850
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002974067"
FT   DOMAIN          80..404
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          445..652
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          687..837
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
SQ   SEQUENCE   850 AA;  90268 MW;  CE10C3466D7393C5 CRC64;
     MKTSSALKLV SLCVLGGVMT GCVKASDVQK VSDQGAAFTE LAASTQESGV ANPDIWPDLA
     PLPLDPEVEA RVDELLAQMT LEQKVGQVIQ GDSDSITPED VKKYRLGSIL SGGSSAPGDK
     AYTDAQTWLD TADAFYDASV DPEGVEVAIP LIWGIDAVHG HTNLAGAVVF PHNIGLGAAN
     NPDLIEKIAA STAKALTISG HDWTFAPTLA VPRDARWGRT YEGFSQSPEI VSEYSARIVE
     GLQGVYGADD FMTEGRVISS AKHFLGDGGT ENGVDQGNVT ISEEELRDIH GAGYIGAVES
     GVQTIMASFN AWHGKKMHGN KSLLTGVLKE QMNFQGFIVG DWNGHGQIAG CTNTDCPQAI
     NAGLDMYMAP DSWKGLWETT LAYAKNGTIP MERLDDAVRR ILRVKIASGI FEKGRPSERA
     NAGDAANLGA DEHRAIAREA VRESLVLIKN NDQILPLAAA QTVMVVGDGA DSISKASGGW
     TLSWQGTGHT NDEFPNGTSI LDGIKSVVEA GGGKVIFNPT GEVMDEKADV VIAVYGEDPY
     AEFQGDIEHL AFLDNGFDTS SLKAHKDAGA KIVSVFLSGR PLWVNNQVNA SDAFIAAWLP
     GSEGDGVADM LFRTSDEFEF TGRLSYPWPN TANAKDALES EPLFNIGYGL TYAENKTLAA
     LSEDAGIALS SQGERGQLFV KGKTVDPWSF VSMSANGVTS IGPEGLQSDL LNVTRADFSA
     QEDALAIEWK EANSRVLTGF VSNAPVDYMR ESNGAMELAF MLRSLSDTNA KLDVLVGCET
     GACEVVSTID APADEWSETR ISLSCFAEKG VSMSNLRSIL ALNASSPSKI GLANVRLEAD
     ADGVQTCPKE
//
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