ID   BGLX_SALTY              Reviewed;         765 AA.
AC   Q56078;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Periplasmic beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
DE   AltName: Full=T-cell inhibitor;
DE   Flags: Precursor;
GN   Name=bglX; OrderedLocusNames=STM2166;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Matsui K.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; D86507; BAA13102.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21070.1; -; Genomic_DNA.
DR   RefSeq; NP_461111.1; NC_003197.2.
DR   RefSeq; WP_000871560.1; NC_003197.2.
DR   AlphaFoldDB; Q56078; -.
DR   SMR; Q56078; -.
DR   STRING; 99287.STM2166; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PaxDb; Q56078; -.
DR   PRIDE; Q56078; -.
DR   EnsemblBacteria; AAL21070; AAL21070; STM2166.
DR   GeneID; 1253688; -.
DR   KEGG; stm:STM2166; -.
DR   PATRIC; fig|99287.12.peg.2292; -.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   OMA; TLITDWD; -.
DR   PhylomeDB; Q56078; -.
DR   BioCyc; SENT99287:STM2166-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 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   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; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..765
FT                   /note="Periplasmic beta-glucosidase"
FT                   /id="PRO_0000011782"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
FT   CONFLICT        630
FT                   /note="R -> L (in Ref. 1; BAA13102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        634..635
FT                   /note="EA -> KP (in Ref. 1; BAA13102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        656
FT                   /note="V -> F (in Ref. 1; BAA13102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="E -> K (in Ref. 1; BAA13102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        717
FT                   /note="E -> K (in Ref. 1; BAA13102)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   765 AA;  83392 MW;  C7C767E6CAC96786 CRC64;
     MKWLCSVGVA VSLAMQPALA ENLFGNHPLT PEARDAFVTD LLKKMTVDEK IGQLRLISVG
     PDNPKEAIRE MIKDGQVGAI FNTVTRQDIR QMQDQVMALS RLKIPLFFAY DVVHGQRTVF
     PISLGLASSF NLDAVRTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRA SEGFGEDTYL
     TSIMGETMVK AMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSSQ RLFNDYMPPY
     KAGLDAGSGA VMVALNSLNG TPATSDSWLL KDVLRDEWGF KGITVSDHGA IKELIKHGTA
     ADPEDAVRVA LKAGVDMSMA DEYYSKYLPG LIKSGKVTMA ELDDATRHVL NVKYDMGLFN
     DPYSHLGPKE SDPVDTNAES RLHRKEAREV ARESVVLLKN RLETLPLKKS GTIAVVGPLA
     DSQRDVMGSW SAAGVANQSV TVLAGIQNAV GDGAKILYAK GANITNDKGI VDFLNLYEEA
     VKIDPRSPQA MIDEAVQAAK QADVVVAVVG ESQGMAHEAS SRTNITIPQS QRDLITALKA
     TGKPLVLVLM NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPISFP
     RSVGQIPVYY SHLNTGRPYN PEKPNKYTSR YFDEANGPLY PFGYGLSYTT FTVSDVTLSS
     PTMQRDGKVT ASVEVTNTGK REGATVIQMY LQDVTASMSR PVKQLKGFEK ITLKPGERKT
     VSFPIDIEAL KFWNQQMKYD AEPGKFNVFI GVDSARVKQG SFELL