ID   BGLX_ECOLI              Reviewed;         765 AA.
AC   P33363; Q2MAU7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   02-SEP-2026, entry version 169.
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   Flags: Precursor;
GN   Name=bglX; Synonyms=yohA; OrderedLocusNames=b2132, JW2120;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Yang M., Luoh S., Goddard A., Reilly D., Henzel W., Bass S.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U15049; AAB38487.1; -; Genomic_DNA.
DR   EMBL; U00007; AAA60495.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75193.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76609.1; -; Genomic_DNA.
DR   PIR; C64981; C64981.
DR   RefSeq; NP_416636.1; NC_000913.3.
DR   RefSeq; WP_000871504.1; NZ_CP009789.1.
DR   AlphaFoldDB; P33363; -.
DR   SMR; P33363; -.
DR   BioGRID; 4260451; 49.
DR   DIP; DIP-9218N; -.
DR   FunCoup; P33363; 271.
DR   IntAct; P33363; 16.
DR   STRING; 511145.b2132; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   jPOST; P33363; -.
DR   PaxDb; 511145-b2132; -.
DR   EnsemblBacteria; AAC75193; AAC75193; b2132.
DR   GeneID; 946682; -.
DR   KEGG; ecj:JW2120; -.
DR   KEGG; eco:b2132; -.
DR   KEGG; ecoc:C3026_11955; -.
DR   PATRIC; fig|511145.12.peg.2212; -.
DR   EchoBASE; EB1951; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   InParanoid; P33363; -.
DR   OMA; MSAYHSY; -.
DR   OrthoDB; 9781691at2; -.
DR   PhylomeDB; P33363; -.
DR   BioCyc; EcoCyc:EG12013-MONOMER; -.
DR   BioCyc; MetaCyc:EG12013-MONOMER; -.
DR   PRO; PR:P33363; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P33363; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:EcoliWiki.
DR   GO; GO:0015926; F:glucosidase activity; IDA:EcoliWiki.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR   FunFam; 2.60.40.10:FF:000495; Periplasmic beta-glucosidase; 1.
DR   FunFam; 3.20.20.300:FF:000005; Periplasmic beta-glucosidase; 1.
DR   FunFam; 3.40.50.1700:FF:000004; Periplasmic beta-glucosidase; 1.
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; IPR051915; Cellulose_Degrad_GH3.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR017853; GH_hydrolase_sf.
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; IPR013783; Ig-like_fold.
DR   NCBIfam; NF011678; PRK15098.1; 1.
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; 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_0000011781"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   765 AA;  83460 MW;  0E89B0AB42B8F8F3 CRC64;
     MKWLCSVGIA VSLALQPALA DDLFGNHPLT PEARDAFVTE LLKKMTVDEK IGQLRLISVG
     PDNPKEAIRE MIKDGQVGAI FNTVTRQDIR AMQDQVMELS RLKIPLFFAY DVLHGQRTVF
     PISLGLASSF NLDAVKTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRA SEGFGEDTYL
     TSTMGKTMVE AMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSPQ RLFNDYMPPY
     KAGLDAGSGA VMVALNSLNG TPATSDSWLL KDVLRDQWGF KGITVSDHGA IKELIKHGTA
     ADPEDAVRVA LKSGINMSMS DEYYSKYLPG LIKSGKVTMA ELDDAARHVL NVKYDMGLFN
     DPYSHLGPKE SDPVDTNAES RLHRKEAREV ARESLVLLKN RLETLPLKKS ATIAVVGPLA
     DSKRDVMGSW SAAGVADQSV TVLTGIKNAV GENGKVLYAK GANVTSDKGI IDFLNQYEEA
     VKVDPRSPQE MIDEAVQTAK QSDVVVAVVG EAQGMAHEAS SRTDITIPQS QRDLIAALKA
     TGKPLVLVLM NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPMSFP
     RSVGQIPVYY SHLNTGRPYN ADKPNKYTSR YFDEANGALY PFGYGLSYTT FTVSDVKLSA
     PTMKRDGKVT ASVQVTNTGK REGATVVQMY LQDVTASMSR PVKQLKGFEK ITLKPGETQT
     VSFPIDIEAL KFWNQQMKYD AEPGKFNVFI GTDSARVKKG EFELL
//