Difference between revisions of "PsdS"

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[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:55, 2 February 2011

  • Description: two-component sensor kinase, control of psdA-psdB in response to lipid II-binding lantibiotics, such as nisin and gallidermin

Gene name psdS
Synonyms yvcQ
Essential no
Product two-component sensor kinase
Function resistance against toxic peptides
MW, pI 40 kDa, 7.358
Gene length, protein length 1068 bp, 356 aa
Immediate neighbours psdA, psdR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvcQ context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

protein modification, transcription factors and their control, resistance against toxins/ antibiotics, membrane proteins, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU34710

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of PsdR
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: two transmembrane segments, C-terminal histidine phosphotransferase domain
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • 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

Stéphanie Coumes-Florens, Céline Brochier-Armanet, Annick Guiseppi, François Denizot, Maryline Foglino
A new highly conserved antibiotic sensing/resistance pathway in firmicutes involves an ABC transporter interplaying with a signal transduction system.
PLoS One: 2011, 6(1);e15951
[PubMed:21283517] [WorldCat.org] [DOI] (I e)

Anna Staroń, Dora Elisabeth Finkeisen, Thorsten Mascher
Peptide antibiotic sensing and detoxification modules of Bacillus subtilis.
Antimicrob Agents Chemother: 2011, 55(2);515-25
[PubMed:21078927] [WorldCat.org] [DOI] (I p)

Eva Rietkötter, Diana Hoyer, Thorsten Mascher
Bacitracin sensing in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);768-85
[PubMed:18394148] [WorldCat.org] [DOI] (I p)

Thorsten Mascher, Neil G Margulis, Tao Wang, Rick W Ye, John D Helmann
Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon.
Mol Microbiol: 2003, 50(5);1591-604
[PubMed:14651641] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)