IseA

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  • Description: inhibits in vitro activity of cell wall endopeptidases LytE and LytF, inhibits cell separation

Gene name iseA
Synonyms yoeB
Essential no
Product inhibitor of autolysins
Function protection against cell envelope stress
Gene expression levels in SubtiExpress: iseA
Interactions involving this protein in SubtInteract: IseA
MW, pI 19 kDa, 10.176
Gene length, protein length 543 bp, 181 aa
Immediate neighbours yoeA, trnSL-Arg1
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YoeB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
IseA expression.png















Categories containing this gene/protein

cell wall degradation/ turnover, membrane proteins

This gene is a member of the following regulons

WalR regulon

The gene

Basic information

  • Locus tag: BSU18380

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:
  • Localization: cell membrane (according to Swiss-Prot), localized to cell separation sites

Database entries

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

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • repressed by WalR PubMed
    • induced by vancomycin PubMed
    • strongly induced in response to glucose starvation in M9 medium 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

Additional publications: PubMed

Ryoichi Arai, Sadaharu Fukui, Naoya Kobayashi, Junichi Sekiguchi
Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis, reveals a novel fold with a characteristic inhibitory loop.
J Biol Chem: 2012, 287(53);44736-48
[PubMed:23091053] [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)

Hiroki Yamamoto, Masayuki Hashimoto, Yuhei Higashitsuji, Hiroyuki Harada, Nozomi Hariyama, Lisa Takahashi, Tomoaki Iwashita, Seika Ooiwa, Junichi Sekiguchi
Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis.
Mol Microbiol: 2008, 70(1);168-82
[PubMed:18761694] [WorldCat.org] [DOI] (I p)

Paola Bisicchia, David Noone, Efthimia Lioliou, Alistair Howell, Sarah Quigley, Thomas Jensen, Hanne Jarmer, Kevin M Devine
The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis.
Mol Microbiol: 2007, 65(1);180-200
[PubMed:17581128] [WorldCat.org] [DOI] (P p)

Letal I Salzberg, John D Helmann
An antibiotic-inducible cell wall-associated protein that protects Bacillus subtilis from autolysis.
J Bacteriol: 2007, 189(13);4671-80
[PubMed:17483219] [WorldCat.org] [DOI] (P p)