Difference between revisions of "PsdR"
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| [[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 08:49, 30 May 2012
-  Description: two-component response regulator, induction of psdA-psdB in response to lipid II-binding lantibiotics, such as nisin and gallidermin 
| Gene name | psdR | 
| Synonyms | yvcP | 
| Essential | no | 
| Product | two-component response regulator | 
| Function | resistance against toxic peptides | 
| Interactions involving this protein in SubtInteract: PsdR | |
| MW, pI | 27 kDa, 4.676 | 
| Gene length, protein length | 711 bp, 237 aa | 
| Immediate neighbours | psdS, yvcN | 
| Get the DNA and protein sequences (Barbe et al., 2009) | |
| Genetic context    This image was kindly provided by SubtiList | |
| Expression at a glance   PubMed   | |
Contents
Categories containing this gene/protein
transcription factors and their control, resistance against toxins/ antibiotics, phosphoproteins
This gene is a member of the following regulons
The PsdR regulon: psdA-psdB
The gene
Basic information
- Locus tag: BSU34720
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: OmpR family of two-component response regulators
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated by PsdS on an Asp residue
- Cofactor(s):
- Effectors of protein activity: phosphorylation likely affects DNA-binding activity
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O06978
- 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
Additional publications: PubMed
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)

