Difference between revisions of "PsdR"
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<pubmed>10094672,18394148,14651641</pubmed> | <pubmed>10094672,18394148,14651641</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:50, 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
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)