Difference between revisions of "YorK"
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=Biological materials = | =Biological materials = |
Revision as of 08:09, 16 April 2012
- Description: single-strand DNA-specific exonuclease
Gene name | yorK |
Synonyms | |
Essential | no |
Product | single-strand DNA-specific exonuclease |
Function | unknown |
Interactions involving this protein in SubtInteract: YorK | |
MW, pI | 65 kDa, 6.562 |
Gene length, protein length | 1728 bp, 576 aa |
Immediate neighbours | yorL, yorJ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
DNA repair/ recombination, SP-beta prophage, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU20350
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: RecJ family
- Paralogous protein(s): YrvE
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Tyr-473 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: O31903
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
V A Sutera, E S Han, L A Rajman, S T Lovett
Mutational analysis of the RecJ exonuclease of Escherichia coli: identification of phosphoesterase motifs.
J Bacteriol: 1999, 181(19);6098-102
[PubMed:10498723]
[WorldCat.org]
[DOI]
(P p)