Difference between revisions of "PsdR"
| 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''' || | + | |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 [[ | + | * '''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:''' [[ | + | * '''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 
This image was kindly provided by SubtiList
| |
Contents
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
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)
