YaaT

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  • Description: control of the phosphorelay, required for the achieving a sufficient level of Spo0A-P for sporulation initiation

Gene name yaaT
Synonyms
Essential no
Product part of the YaaT-YmcA-YlbF complex
Function regulation of sporulation initiation
Gene expression levels in SubtiExpress: yaaT
Interactions involving this protein in SubtInteract: YaaT
MW, pI 31 kDa, 4.838
Gene length, protein length 825 bp, 275 aa
Immediate neighbours holB, yabA
Sequences Protein DNA DNA_with_flanks
Genetic context
YaaT context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YaaT expression.png















Categories containing this gene/protein

phosphorelay, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00320

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • expressed during growth and the transition phase, expression is erduced in stationary phase PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Valerie J Carabetta, Andrew W Tanner, Todd M Greco, Melissa Defrancesco, Ileana M Cristea, David Dubnau
A complex of YlbF, YmcA and YaaT regulates sporulation, competence and biofilm formation by accelerating the phosphorylation of Spo0A.
Mol Microbiol: 2013, 88(2);283-300
[PubMed:23490197] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Shigeo Hosoya, Kei Asai, Naotake Ogasawara, Michio Takeuchi, Tsutomu Sato
Mutation in yaaT leads to significant inhibition of phosphorelay during sporulation in Bacillus subtilis.
J Bacteriol: 2002, 184(20);5545-53
[PubMed:12270811] [WorldCat.org] [DOI] (P p)