PsdR

• 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

Categories containing this gene/protein

transcription factors and their control, resistance against toxins/ antibiotics, phosphoproteins

The gene

Basic information

• Locus tag: BSU34720

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• Interactions:
  • PsdR-PsdS

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: O06978

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: psdR-psdS-psdA-psdB PubMed

• Expression browser: psdR PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

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)