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Database: UniProt
Entry: A6WBM4_KINRD
LinkDB: A6WBM4_KINRD
Original site: A6WBM4_KINRD 
ID   A6WBM4_KINRD            Unreviewed;       670 AA.
AC   A6WBM4;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   OrderedLocusNames=Krad_2741 {ECO:0000313|EMBL:ABS04213.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS04213.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) 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; CP000750; ABS04213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6WBM4; -.
DR   STRING; 266940.Krad_2741; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; kra:Krad_2741; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_8_2_11; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000001116; 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; 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; 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; IPR006311; TAT_signal.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 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; PS51318; TAT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABS04213.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116}.
FT   DOMAIN          124..380
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          538..667
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   670 AA;  70776 MW;  A6E6CB3808F0FD6E CRC64;
     MDGHPRTPRP SRSRRRVSRA AAALAGLVAV TIGGTTTSSA TPAAPPGRAG DQPVLSTRGV
     ELLRIGGLQF RDLDRDGRLT PYEDWRLSPA QRADDLLGRL DLAQRAGLLV HGNLASSGTT
     YDVAATVRDV ADRHVTTFIT RLSAEPAQIA EANNLVQLIA EQQPLAIPVL VSSDPRNGFS
     ETEGQTVAGE GTTSLPDPTG LSAAGDPDLT RRVGDVVRQE FRAMGIAELL GPQADLATEP
     RWTRIDGTFG SDAATARDQV GAYVDGVQGG TAGLDRDSVA TVTKHWAGYG AQVDGYDSHY
     HYGRYAAFPG GNFEEHLLPY DGAFAAGTAG IMPTYSILQG LQREGHDVEQ VGAGFNSYLL
     QDVLRGEKGF DGVVLSDWGI TGDCPQECLD NRPPNRFVGS WGVGMPWGME DATRTERFAK
     ALNAGVDQIG GDSDSTQVVA AVEQGLLSAD RVAQAAHRVL VQKFQLGLFE NPFVDPATAD
     RIAGNARFQR IGDEAQEKSL TLLQNTDDLL PVSRASVRTV YLAGVDPAVA RSRGLAVTDD
     PAEADLAIVR IADPRSGTDL TGLEPTEEQE DVRLLQAAAA AGTPTVAVPK LARPLILTGV
     VATADAVLAN YGVSDEVLLD TVLGRRAPGG RLPFELPSST AAVEAQLPDV ADDSADPLFA
     RGAGLSYDRR
//
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