GlcT

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Gene name glcT
Synonyms ykwA
Essential no
Product transcriptional antiterminator of the ptsG-ptsH-ptsI operon
Function control of glucose uptake
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

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

  • KEGG entry: [2]

Additional information

Expression and regulation

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

Biological materials

  • Mutant: available in Stülke lab:
    • GP109 (in frame deletion)
    • GP778 (replacement of glcT and the ptsGHI operon by a spc cassette)
    • GP926 (substitution of glct and ptsG by a tet cassette)
  • 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

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol. Microbiol.: 2008, 67(4);692-702
[PubMed:18086213] [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] (P p)

Original publications

Dayté D Rodríguez, Christian Grosse, Sebastian Himmel, César González, Iñaki M de Ilarduya, Stefan Becker, George M Sheldrick, Isabel Usón
Crystallographic ab initio protein structure solution below atomic resolution.
Nat. Methods: 2009, 6(9);651-3
[PubMed:19684596] [WorldCat.org] [DOI] (I p)

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] (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] (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] (P p)