ID   E0I868_9BACL            Unreviewed;       880 AA.
AC   E0I868;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=PaecuDRAFT_1819 {ECO:0000313|EMBL:EFM11373.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11373.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM11373.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM11373.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-2010) 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; AEDD01000004; EFM11373.1; -; Genomic_DNA.
DR   RefSeq; WP_006037830.1; NZ_AEDD01000004.1.
DR   AlphaFoldDB; E0I868; -.
DR   STRING; 717606.PaecuDRAFT_1819; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000005387; 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; 2.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
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   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFM11373.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT   DOMAIN          486..625
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   880 AA;  96683 MW;  BA97EACC65E8E5CC CRC64;
     MAEPTLSTAL YRNPEAPIDD RVHDLLTRMT LQEKVRQLDQ YFGTSFVSAT HPHMITVMAE
     DATVDWDKVK SVIGEDGIGC IHDLYGTADM NNTLQRYAVE ETRLGIPILF SEEALHGLLR
     PGMTVYPHAI AMASTWNPEL VKQIGRDIAA ETRSLGIHES FGPVLDLARD PRWGRVEETF
     GEDTHLASRM GVAMVQGLQG DSLDATDSII AEPKHFAVHG IPESGLNHSP VSIGANDIRT
     YHLPVFEAAY KEGGAINAMC AYHAMDGVPC ASDYDLLTGI LRDEWQMPGF VRSDLGAIAR
     LEHAHGTADS DKEAIRQALV AGVDMQYYDY PHDVYQNAIV EMVQSGELLE ETLDLAVIRV
     LKVKFMLGLF EKPYAVPGLS ERVVRSEEHL QTALQAAREA ICLLQNEGSL LPLRKEIGTI
     AVIGPSADKA RLGDYTPYIE GFQPSTVLQG IAQAVSSQTR VLHAKGTGIL DGELEPIPMG
     SFREPNGGEG LKGEYFNNET LEGEPALVRN DPHIHFNWAI TKADQQLKSY GFSVRWTGKL
     VPQMSFSGYI GTVTQDSMRL WLDGELLVDG WGKDKRASVS VPIELQSGRE YDLRVEYVKD
     MNGVDITLGW SRDEEGIQEA VELARQADVA IIALGDSERT CGEGVDRSSL DLPGNQLRLL
     KAIHETGTPV VLVLQNGRPI TLDWESQHIP AIVEVWYGGE RAGEAIAEVL FGDYNPAGRL
     PISFPRTIGQ IPVCYNKRRG GQKHYVGGDN KPLYAFGHGL SYTTFRYANL RVDKSVIAPD
     ESVVVTMDVT NDGNVAGDEV VQLYVVDPVA SVAMPEKQLR HFARIALQPG ETRTVSFTVT
     PRDLALVNKQ LAWVVELGEF TLQVGPSSDQ VALEARITVA
//