Difference between revisions of "PsdR"

From SubtiWiki
Jump to: navigation, search
m (moved YvcP to PsdR: 21078927)
Line 1: Line 1:
* '''Description:''' [[two-component systems|two-component]] response regulator <br/><br/>
+
* '''Description:''' [[two-component systems|two-component]] response regulator, induction of ''[[psdA]]-[[psdB]]'' in response to lipid II-binding lantibiotics, such as nisin and gallidermin <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
Line 12: Line 12:
 
|style="background:#ABCDEF;" align="center"| '''Product''' || [[two-component systems|two-component]] response regulator  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || [[two-component systems|two-component]] response regulator  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
+
|style="background:#ABCDEF;" align="center"|'''Function''' || resistance against toxic peptides
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 4.676   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 4.676   
Line 64: Line 64:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:''' phosphorylated by [[YvcQ]] on an Asp residue
+
* '''Modification:''' phosphorylated by [[PsdS]] on an Asp residue
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
Line 70: Line 70:
 
* '''Effectors of protein activity:''' phosphorylation likely affects DNA-binding activity
 
* '''Effectors of protein activity:''' phosphorylation likely affects DNA-binding activity
  
* '''Interactions:''' [[YvcQ]]-[[YvcP]]
+
* '''Interactions:''' [[PsdR]]-[[PsdS]]
  
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
Line 88: Line 88:
 
=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
+
* '''Operon:''' ''[[psdR]]-[[psdS]]-[[psdA]]-[[psdB]]'' {{PubMed|21078927}}
  
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|21078927}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 118: Line 118:
 
=References=
 
=References=
  
<pubmed>10094672,18394148,14651641,, </pubmed>
+
<pubmed>10094672,18394148,14651641,21078927, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:22, 17 November 2010

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

Gene name yvcP
Synonyms
Essential no
Product two-component response regulator
Function resistance against toxic peptides
MW, pI 27 kDa, 4.676
Gene length, protein length 711 bp, 237 aa
Immediate neighbours yvcQ, yvcN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvcP context.gif
This image was kindly provided by SubtiList



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:
  • 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

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)