Difference between revisions of "GlcT"

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(Biological materials)
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* '''Description:''' Transcriptional antiterminator, controls expression of the ''ptsGHI'' operon<br/><br/>
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* '''Description:''' Transcriptional antiterminator, controls expression of the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon<br/><br/>
  
 
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
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|style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional antiterminator of the ''ptsGHI'' operon
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|style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional antiterminator of the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || transcriptional antiterminator  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || transcriptional antiterminator  

Revision as of 15:44, 2 September 2009

  • Description: Transcriptional antiterminator, controls expression of the ptsG-ptsH-ptsI operon

Gene name glcT
Synonyms ykwA
Essential no
Product transcriptional antiterminator of the ptsG-ptsH-ptsI operon
Function transcriptional antiterminator
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 33,0 kDa, 7.01
Gene length, protein length 855 bp, 285 amino acids
Immediate neighbours ykvZ, ptsG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlcT context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU13880

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcriptional antiterminator, RNA-binding protein, binds the ptsG RAT sequence
  • Protein family: antiterminator of the BglG/ SacY family

Extended information on the protein

  • Kinetic information:
  • Domains:
    • RNA-binding domain (N-terminal, constitutive antiterminator)
    • 2x PTS regulation domains (PRDs) (C-terminal, neg. regulated by PtsG)
  • Modification: phosphorylation (His104)
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP109 (in frame deletion), available in Stülke lab
  • Expression vector:
    • pGP124 (full length, in pWH844), available in Stülke lab
    • pGP114 (amino acids 1-60, RNA-binding domain, in pWH844), available in Stülke lab
    • pGP230 (amino acids 1-60, RNA-binding domain with thrombin cleavage site, in pWH844), available in Stülke lab
    • pGP164 (both PRDs, in pWH844), in addition diverse expression vectors for phosphorylation site mutants and for RBD mutants (all in pWH844), available in Stülke lab
    • pGP424 (PRDI, in pWH844), available in Stülke lab
    • pGP425 (PRDII, in pWH844), available in Stülke lab
    • pGP442 (PRDI, in pGP570, with thrombin cleavage site), available in Stülke lab
    • pGP443 (PRDII, in pGP570, with thrombin cleavage site), available in Stülke lab
    • pGP575 (amino acids 1-60, RNA-binding domain with Strep-tag, in pGP574), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Oliver Schilling, Christina Herzberg, Tina Hertrich, Hanna Vörsmann, Dirk Jessen, Sebastian Hübner, Fritz Titgemeyer, Jörg Stülke
Keeping signals straight in transcription regulation: specificity determinants for the interaction of a family of conserved bacterial RNA-protein couples.
Nucleic Acids Res: 2006, 34(21);6102-15
[PubMed:17074746] [WorldCat.org] [DOI] (I p)

Oliver Schilling, Ines Langbein, Michael Müller, Matthias H Schmalisch, Jörg Stülke
A protein-dependent riboswitch controlling ptsGHI operon expression in Bacillus subtilis: RNA structure rather than sequence provides interaction specificity.
Nucleic Acids Res: 2004, 32(9);2853-64
[PubMed:15155854] [WorldCat.org] [DOI] (I e)

Matthias H Schmalisch, Steffi Bachem, Jörg Stülke
Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT.
J Biol Chem: 2003, 278(51);51108-15
[PubMed:14527945] [WorldCat.org] [DOI] (P p)

David B Greenberg, Jorg Stülke, Milton H Saier
Domain analysis of transcriptional regulators bearing PTS regulatory domains.
Res Microbiol: 2002, 153(8);519-26
[PubMed:12437213] [WorldCat.org] [DOI] (P p)

I Langbein, S Bachem, J Stülke
Specific interaction of the RNA-binding domain of the bacillus subtilis transcriptional antiterminator GlcT with its RNA target, RAT.
J Mol Biol: 1999, 293(4);795-805
[PubMed:10543968] [WorldCat.org] [DOI] (P p)

S Bachem, J Stülke
Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system.
J Bacteriol: 1998, 180(20);5319-26
[PubMed:9765562] [WorldCat.org] [DOI] (P p)

J Stülke, M Arnaud, G Rapoport, I Martin-Verstraete
PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Mol Microbiol: 1998, 28(5);865-74
[PubMed:9663674] [WorldCat.org] [DOI] (P p)

J Stülke, I Martin-Verstraete, M Zagorec, M Rose, A Klier, G Rapoport
Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT.
Mol Microbiol: 1997, 25(1);65-78
[PubMed:11902727] [WorldCat.org] [DOI] (P p)