BGLG_ECOLI
ID BGLG_ECOLI Reviewed; 278 AA.
AC P11989; Q2M841; Q47078;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cryptic beta-glucoside bgl operon antiterminator;
GN Name=bglG; Synonyms=bglC; OrderedLocusNames=b3723, JW3701;
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;
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 1-197.
RC STRAIN=K12;
RX PubMed=3301003; DOI=10.1016/0092-8674(87)90502-2;
RA Mahadevan S., Wright A.;
RT "A bacterial gene involved in transcription antitermination: regulation at
RT a rho-independent terminator in the bgl operon of E. coli.";
RL Cell 50:485-494(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 264-278.
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 [7]
RP REGULATION BY PHOSPHORYLATION.
RX PubMed=2200123; DOI=10.1126/science.2200123;
RA Amster-Choder O., Wright A.;
RT "Regulation of activity of a transcriptional anti-terminator in E. coli by
RT phosphorylation in vivo.";
RL Science 249:540-542(1990).
RN [8]
RP REGULATION BY PHOSPHORYLATION.
RX PubMed=2195546; DOI=10.1073/pnas.87.13.5074;
RA Schnetz K., Rak B.;
RT "Beta-glucoside permease represses the bgl operon of Escherichia coli by
RT phosphorylation of the antiterminator protein and also interacts with
RT glucose-specific enzyme III, the key element in catabolite control.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5074-5078(1990).
RN [9]
RP RNA-BINDING.
RX PubMed=1698125; DOI=10.1016/0092-8674(90)90392-r;
RA Houman F., Diaz-Torre M.R., Wright A.;
RT "Transcriptional antitermination in the bgl operon of E. coli is modulated
RT by a specific RNA binding protein.";
RL Cell 62:1153-1163(1990).
CC -!- FUNCTION: Mediates the positive regulation of the beta-glucoside (bgl)
CC operon by functioning as a transcriptional antiterminator. This is an
CC RNA-binding protein that recognizes a specific sequence located just
CC upstream of two termination sites within the operon.
CC -!- INTERACTION:
CC P11989; P06710: dnaX; NbExp=3; IntAct=EBI-545674, EBI-549140;
CC P11989; P0AA04: ptsH; NbExp=5; IntAct=EBI-545674, EBI-902853;
CC P11989; P08839: ptsI; NbExp=3; IntAct=EBI-545674, EBI-551533;
CC P11989; P77700: yahB; NbExp=4; IntAct=EBI-545674, EBI-545731;
CC -!- PTM: Phosphorylated and inactivated by BglF (eII-bgl). The degree of
CC phosphorylation is dependent on the presence or absence of beta-
CC glucosides which act as inducers of the operon expression. Addition of
CC inducer result in the rapid dephosphorylation of BglG.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC {ECO:0000305}.
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DR EMBL; M16487; AAA23509.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62074.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76746.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77565.1; -; Genomic_DNA.
DR EMBL; M17098; AAA23512.1; -; Genomic_DNA.
DR EMBL; M15746; AAA83836.1; ALT_SEQ; Genomic_DNA.
DR PIR; B25977; B25977.
DR RefSeq; NP_418179.1; NC_000913.3.
DR RefSeq; WP_001295251.1; NZ_SSZK01000036.1.
DR AlphaFoldDB; P11989; -.
DR SMR; P11989; -.
DR BioGRID; 4262138; 6.
DR BioGRID; 852537; 7.
DR DIP; DIP-9216N; -.
DR IntAct; P11989; 14.
DR MINT; P11989; -.
DR STRING; 511145.b3723; -.
DR PaxDb; P11989; -.
DR PRIDE; P11989; -.
DR EnsemblBacteria; AAC76746; AAC76746; b3723.
DR EnsemblBacteria; BAE77565; BAE77565; BAE77565.
DR GeneID; 948235; -.
DR KEGG; ecj:JW3701; -.
DR KEGG; eco:b3723; -.
DR PATRIC; fig|1411691.4.peg.2978; -.
DR EchoBASE; EB0114; -.
DR eggNOG; COG3711; Bacteria.
DR HOGENOM; CLU_078802_0_0_6; -.
DR InParanoid; P11989; -.
DR OMA; VMQEILN; -.
DR PhylomeDB; P11989; -.
DR BioCyc; EcoCyc:EG10116-MON; -.
DR PHI-base; PHI:4630; -.
DR PRO; PR:P11989; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.30.24.10; -; 1.
DR InterPro; IPR004341; CAT_RNA-bd_dom.
DR InterPro; IPR036650; CAT_RNA-bd_dom_sf.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR001550; Transcrpt_antitermin_CS.
DR Pfam; PF03123; CAT_RBD; 1.
DR Pfam; PF00874; PRD; 2.
DR SMART; SM01061; CAT_RBD; 1.
DR SUPFAM; SSF50151; SSF50151; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS00654; PRD_1; 1.
DR PROSITE; PS51372; PRD_2; 2.
PE 1: Evidence at protein level;
KW Activator; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..278
FT /note="Cryptic beta-glucoside bgl operon antiterminator"
FT /id="PRO_0000204244"
FT DOMAIN 67..171
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 172..278
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
SQ SEQUENCE 278 AA; 32097 MW; 5ACF1A14BF438B4F CRC64;
MNMQITKILN NNVVVVIDDQ QREKVVMGRG IGFQKRAGER INSSGIEKEY ALSSHELNGR
LSELLSHIPL EVMATCDRII SLAQERLGKL QDSIYISLTD HCQFAIKRFQ QNVLLPNPLL
WDIQRLYPKE FQLGEEALTI IDKRLGVQLP KDEVGFIAMH LVSAQMSGNM EDVAGVTQLM
REMLQLIKFQ FSLNYQEESL SYQRLVTHLK FLSWRILEHA SINDSDESLQ QAVKQNYPQA
WQCAERIAIF IGLQYQRKIS PAEIMFLAIN IERVRKEH
