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Database: UniProt
Entry: M5CP88_STEMA
LinkDB: M5CP88_STEMA
Original site: M5CP88_STEMA 
ID   M5CP88_STEMA            Unreviewed;       954 AA.
AC   M5CP88;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:CCP12159.1};
DE            EC=3.2.1.21 {ECO:0000313|EMBL:CCP12159.1};
GN   Name=bglS {ECO:0000313|EMBL:CCP12159.1};
GN   ORFNames=SMSKK35_1446 {ECO:0000313|EMBL:CCP12159.1};
OS   Stenotrophomonas maltophilia SKK35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=1118156 {ECO:0000313|EMBL:CCP12159.1, ECO:0000313|Proteomes:UP000012178};
RN   [1] {ECO:0000313|EMBL:CCP12159.1, ECO:0000313|Proteomes:UP000012178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKK35 {ECO:0000313|EMBL:CCP12159.1,
RC   ECO:0000313|Proteomes:UP000012178};
RA   Linke B., Adamek M., Schwartz T.;
RT   "Stenotrophomonas maltophilia SKK35 and RA8 genome sequencing: analysis and
RT   comparison of viurlence genes.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCP12159.1}.
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DR   EMBL; CALN01000912; CCP12159.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5CP88; -.
DR   Proteomes; UP000012178; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 2.
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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           48..954
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004064604"
FT   DOMAIN          869..937
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   954 AA;  100693 MW;  8EF6864A2730159E CRC64;
     MNAAPFGGTF PGPIALATEL RLPMKTFTKP LALSLALSAA LAAPAWADPA AFTVLTLEQA
     PGAEAMPALA AQLKSLKVDA VSVRQVQRGI GQVDPLQVLA DGLGYEYRFI AAGKDDGQTQ
     RGQAVLTRLP IAAESGPDQP GLNYLRLDDG RHTVAVYTDA GAGAAQLPAL VTRSRLGAPA
     VLLGAVAGES ATAAGFDPAR VALEADASYF SDGFQAASSA PFKVEGSSLR ATLLTLAYAA
     DTHGDTPWMD TTLNADARAA LLLKAMTEDE KFQMLHSYFG LGKDGGPLPE GAVGSAGFVP
     AVPRLGIPSQ QSADAGVGVT NPGGIRPGDF ATAMPSGPST ASSWNREVAF AGGATMGREA
     WQQRFNILLS GSVNLQRDPR NGRNFEYAGE DPLLAGSMVG ALIQGVQSQH VISSMKHFAL
     NDMETRRNFH DVRIGEQAMH ESDLLAFEIA LEAGRPGVAM CSYNKINGTY GCENGYLMNQ
     VLKQEWKFPG FVMSDWGGVH SGSKAALAGL DQQSAGEVFD AAVFFDEPLR LAVHGGVVPQ
     ARLNDMVARI LRTMFLHGNF DNPPQHQKVD AEAGFAVAQR TVEEGSVLLR NEGNLLPLAD
     SVKRIVIIGG HADKGVIGGG GSSMVGVTAK GTNAVPGVLP TTWPGPVIFH PSSPLESLRA
     ARPDATIEYV DGSNAAAAAK AAAQADVAIV FATQWAAESV DLPDMQLPDN QDALISAVAK
     ANPKTVLVLE TNGPVRTPWL AQVPAMLQAW YPGIRGGEGI AALLTGQVNP SGRLPVTWVV
     DESQLPRPHI DGLGFKPAKP FGDVFDFDIE GANVGYKWMA AKGLTPTFAF GHGLSYTSFA
     YENLKVSVEG SRLVASVDIR NTGKRAGADV AQLYLKLPAG STTPIRLIGY DKVNLQPGEQ
     RRIRIEAEPK TLAHYDAQAR QWKIDGGTYQ VQLSRNAAEP LQSVDVQLVE QVLR
//
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