Difference between revisions of "CtsR"
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− | * '''Structure:''' | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3H0D 3H0D] (complex with a 26bp DNA duplex, from ''Geobacillus stearothermophilus'') {{PubMed|19498169}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37568 P37568] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37568 P37568] |
Revision as of 14:36, 3 February 2010
Gene name | ctsR |
Synonyms | yacG |
Essential | no |
Product | transcription repressor |
Function | regulation of protein degradation |
Regulatory function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 17 kDa, 9.261 |
Gene length, protein length | 462 bp, 154 aa |
Immediate neighbours | rrnW-5S, mcsA |
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: BSU00830
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ctsR family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation of a tyrosine residue by McsB PubMed, recently, it was reported thatCtsR is phosphorylatedby McsB on Arg-62 rather than on a tyrosine residue PubMed
- Cofactor(s):
- Effectors of protein activity: probably activated by dephosphorylation by McsA and inactivated by phosphorylation by McsB PubMed1 PubMed2, regulated proteolysis by ClpP/ClpC PubMed, PubMed, PubMed
- Localization:
Database entries
- UniProt: P37568
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information: the mRNA is very stable (half-life > 15 min) PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References