ID   BGLB_ECOLI              Reviewed;         470 AA.
AC   P11988; P78124; Q2M839;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=6-phospho-beta-glucosidase BglB;
DE            EC=3.2.1.86;
DE   AltName: Full=Phospho-beta-glucosidase B;
GN   Name=bglB; OrderedLocusNames=b3721, JW3699;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYPTIC OPERON.
RC   STRAIN=K12;
RX   PubMed=3034860; DOI=10.1128/jb.169.6.2579-2590.1987;
RA   Schnetz K., Toloczyki C., Rak B.;
RT   "Beta-glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence,
RT   genetic organization, and possible evolutionary relationship to regulatory
RT   components of two Bacillus subtilis genes.";
RL   J. Bacteriol. 169:2579-2590(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC   STRAIN=K12;
RX   PubMed=3309161; DOI=10.1099/00221287-133-3-563;
RA   Bramley H.F., Kornberg H.L.;
RT   "Nucleotide sequence of bglC, the gene specifying enzymeIIbgl of the
RT   PEP:sugar phosphotransferase system in Escherichia coli K12, and
RT   overexpression of the gene product.";
RL   J. Gen. Microbiol. 133:563-573(1987).
RN   [6]
RP   FUNCTION AS A GLUCOSIDASE, AND SUBSTRATE SPECIFICITY.
RX   PubMed=4576407; DOI=10.1128/jb.114.3.909-915.1973;
RA   Prasad I., Young B., Schaefler S.;
RT   "Genetic determination of the constitutive biosynthesis of phospho-
RT   glucosidase A in Escherichia coli K-12.";
RL   J. Bacteriol. 114:909-915(1973).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphorylated beta-glucosides
CC       into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity
CC       for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-
CC       glucoside, phenyl beta-glucoside, arbutin and phosphorylated salicin),
CC       and a low affinity for phosphorylated beta-methyl-glucoside.
CC       {ECO:0000269|PubMed:4576407}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC         D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC   -!- MISCELLANEOUS: Part of the cryptic bglGFBH operon.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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; M16487; AAA23511.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62072.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76744.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77567.1; -; Genomic_DNA.
DR   EMBL; M15746; AAA83838.1; -; Genomic_DNA.
DR   PIR; B65175; B65175.
DR   RefSeq; NP_418177.1; NC_000913.3.
DR   RefSeq; WP_000643228.1; NZ_SSZK01000036.1.
DR   AlphaFoldDB; P11988; -.
DR   SMR; P11988; -.
DR   BioGRID; 4261195; 13.
DR   BioGRID; 852536; 1.
DR   DIP; DIP-9214N; -.
DR   IntAct; P11988; 4.
DR   STRING; 511145.b3721; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; P11988; -.
DR   PRIDE; P11988; -.
DR   EnsemblBacteria; AAC76744; AAC76744; b3721.
DR   EnsemblBacteria; BAE77567; BAE77567; BAE77567.
DR   GeneID; 948234; -.
DR   KEGG; ecj:JW3699; -.
DR   KEGG; eco:b3721; -.
DR   PATRIC; fig|1411691.4.peg.2980; -.
DR   EchoBASE; EB0112; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_6; -.
DR   InParanoid; P11988; -.
DR   OMA; YGGWGSR; -.
DR   PhylomeDB; P11988; -.
DR   BioCyc; EcoCyc:EG10114-MON; -.
DR   BioCyc; MetaCyc:EG10114-MON; -.
DR   SABIO-RK; P11988; -.
DR   PRO; PR:P11988; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IDA:EcoCyc.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISS:UniProtKB.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..470
FT                   /note="6-phospho-beta-glucosidase BglB"
FT                   /id="PRO_0000063898"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        361
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   CONFLICT        147
FT                   /note="D -> G (in Ref. 1; AAA23511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449..451
FT                   /note="GWY -> RMVC (in Ref. 1; AAA23511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   470 AA;  53161 MW;  2B8422B20D7E5C98 CRC64;
     MKAFPETFLW GGATAANQVE GAWQEDGKGI STSDLQPHGV MGKMEPRILG KENIKDVAID
     FYHRYPEDIA LFAEMGFTCL RISIAWARIF PQGDEVEPNE AGLAFYDRLF DEMAQAGIKP
     LVTLSHYEMP YGLVKNYGGW ANRAVIDHFE HYARTVFTRY QHKVALWLTF NEINMSLHAP
     FTGVGLAEES GEAEVYQAIH HQLVASARAV KACHSLLPEA KIGNMLLGGL VYPLTCQPQD
     MLQAMEENRR WMFFGDVQAR GQYPGYMQRF FRDHNITIEM TESDAEDLKH TVDFISFSYY
     MTGCVSHDES INKNAQGNIL NMIPNPHLKS SEWGWQIDPV GLRVLLNTLW DRYQKPLFIV
     ENGLGAKDSV EADGSIQDDY RIAYLNDHLV QVNEAIADGV DIMGYTSWGP IDLVSASHSQ
     MSKRYGFIYV DRDDNGEGSL TRTRKKSFGW YAEVIKTRGL SLKKITIKAP