YaaT
- 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
- block of sporulation at stage 0 PubMed
- strongly reduced genetic competence, strongly reduced sporulation PubMed
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:
- Localization:
- peripheral membrane, as well as to the septum, during sporulation PubMed
Database entries
- Structure:
- UniProt: P37541
- 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)