ID   A0A1W6LPU7_9BACT        Unreviewed;       745 AA.
AC   A0A1W6LPU7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE   Flags: Precursor;
GN   Name=bglX {ECO:0000313|EMBL:ARN57787.1};
GN   ORFNames=STSP1_02213 {ECO:0000313|EMBL:ARN57787.1};
OS   Sedimentisphaera salicampi.
OC   Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC   Sedimentisphaeraceae; Sedimentisphaera.
OX   NCBI_TaxID=1941349 {ECO:0000313|EMBL:ARN57787.1, ECO:0000313|Proteomes:UP000193334};
RN   [1] {ECO:0000313|Proteomes:UP000193334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-PulAB-D4 {ECO:0000313|Proteomes:UP000193334};
RA   Spring S., Bunk B., Sproer C.;
RT   "Comparative genomics and description of representatives of a novel lineage
RT   of planctomycetes thriving in anoxic sediments.";
RL   Submitted (APR-2017) 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};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP021023; ARN57787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6LPU7; -.
DR   STRING; 1941349.STSP1_02213; -.
DR   KEGG; pbp:STSP1_02213; -.
DR   Proteomes; UP000193334; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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; IPR019800; Glyco_hydro_3_AS.
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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:ARN57787.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193334};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..745
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013230060"
FT   DOMAIN          670..739
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   745 AA;  82656 MW;  7DD67D5E4BFDF54B CRC64;
     MGANRNVLKL FSLLLIFTVS LVNAEEKVEK KVDALLSKMT LDEKAGQMTQ LTLKAFTNGK
     SGDKLKLDEN KLEKYIVQEK IGSVLNCGGR ALSPEKWLEI TSLVQKFAKK TRLQIPVIYG
     LDSIHGAGYV AGSTLFPHNI AMAAAGSRQL VQQMAEVTAL ETRAAGIRWN FAPVLGVARH
     PFWPRHYETF GEDPFIASEF AEAYITGLQG DKLPLAEDKV LACMKHFLGY SYPRSGRDRT
     PAWIPEIQLR ELFVPPFRAA VQAGAVTAMI NSSEINGRPV HASPFYLKKL LRKDIGFSGF
     VVSDWADIDN LYTREMVAEN QREAVKIGVN AGIDMSMTPF KIDFKKHLVS LVEAGEVPVQ
     RVDEAVKNII KVKFQAGLFN DPFEDDKLSE KIASKEAKKL NERCAEECIT LLKNESEILP
     LKKEEKILVT GPCSNLKSVL NGGWSRTWQG REEHLYPDSQ NTILEAVKAE FGRGNVSFEK
     GADFDKLLDA DKAAEKAENC DVILLCAGEN TYTEHSGNIR DYNISLSQRK LAARLSETGK
     PIITILTQGR PRVVREIEKV SDAVVMAYLP GVKGADAIAD VVSGDVNPSG RLPFSYPKYA
     GGFEWYDYKK SANWSSCKVE FQWPFGAGLS YTDFECSGLK LSKNSASKKG FDGLKVSFDV
     KNKGKMKGGY IAQVYVSDKV ASVTPANKRL KEFKKIYLNP GENQTVNFDL PAEAFSFINA
     ECRRVIEPGK FIIRAGGLKK EFTLE
//