Difference between revisions of "GerR"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15090&redirect=T BSU15090]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gerR.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gerR.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15090&redirect=T BSU15090]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 13:38, 2 April 2014

  • Description: probably DNA-binding protein, regulates transcription of some spore coat genes

Gene name gerR
Synonyms ylbO
Essential no
Product unknown
Function spore coat formation and resistance of spores to lysozyme
Gene expression levels in SubtiExpress: gerR
MW, pI 22 kDa, 7.109
Gene length, protein length 579 bp, 193 aa
Immediate neighbours rpmF, ylbP
Sequences Protein DNA DNA_with_flanks
Genetic context
YlbO context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GerR expression.png
























Categories containing this gene/protein

transcription factors and their control, sporulation proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

The GerR regulon

The gene

Basic information

  • Locus tag: BSU15090

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

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: phosphorylated on Ser-180 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: gerR (according to DBTBS)
  • Regulation:
    • expressed during sporulation in the mother cell (SigE, SpoIIID) PubMed
    • repressed by glucose (3.2-fold) PubMed
    • repressed by casamino acids PubMed
  • 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

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Giuseppina Cangiano, Antonio Mazzone, Loredana Baccigalupi, Rachele Isticato, Patrick Eichenberger, Maurilio De Felice, Ezio Ricca
Direct and indirect control of late sporulation genes by GerR of Bacillus subtilis.
J Bacteriol: 2010, 192(13);3406-13
[PubMed:20435725] [WorldCat.org] [DOI] (I p)

Ritsuko Kuwana, Takashi Okumura, Hiromu Takamatsu, Kazuhito Watabe
The ylbO gene product of Bacillus subtilis is involved in the coat development and lysozyme resistance of spore.
FEMS Microbiol Lett: 2005, 242(1);51-7
[PubMed:15621419] [WorldCat.org] [DOI] (P p)

Patrick Eichenberger, Masaya Fujita, Shane T Jensen, Erin M Conlon, David Z Rudner, Stephanie T Wang, Caitlin Ferguson, Koki Haga, Tsutomu Sato, Jun S Liu, Richard Losick
The program of gene transcription for a single differentiating cell type during sporulation in Bacillus subtilis.
PLoS Biol: 2004, 2(10);e328
[PubMed:15383836] [WorldCat.org] [DOI] (I p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)