BGLX_ECOLI
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 03-AUG-2022, entry version 154.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_SSZK01000011.1.
DR AlphaFoldDB; P33363; -.
DR SMR; P33363; -.
DR BioGRID; 4260451; 32.
DR DIP; DIP-9218N; -.
DR IntAct; P33363; 16.
DR STRING; 511145.b2132; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR jPOST; P33363; -.
DR PaxDb; P33363; -.
DR PRIDE; P33363; -.
DR EnsemblBacteria; AAC75193; AAC75193; b2132.
DR EnsemblBacteria; BAE76609; BAE76609; BAE76609.
DR GeneID; 946682; -.
DR KEGG; ecj:JW2120; -.
DR KEGG; eco:b2132; -.
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; TLITDWD; -.
DR PhylomeDB; P33363; -.
DR BioCyc; EcoCyc:EG12013-MON; -.
DR BioCyc; MetaCyc:EG12013-MON; -.
DR PRO; PR:P33363; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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: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_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
