Difference between revisions of "PolX"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' monomeric [http://www.ncbi.nlm.nih.gov/sites/entrez/18938175 PubMed] | + | * '''[[SubtInteract|Interactions]]:''' |
| + | ** monomeric [http://www.ncbi.nlm.nih.gov/sites/entrez/18938175 PubMed] | ||
| − | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
Revision as of 20:16, 8 December 2011
- Description: DNA polymerase X, involved in DNA repair
| Gene name | polX |
| Synonyms | yshC |
| Essential | no |
| Product | DNA polymerase X |
| Function | DNA repair |
| MW, pI | 63 kDa, 5.308 |
| Gene length, protein length | 1710 bp, 570 aa |
| Immediate neighbours | mutSB, yshB |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28590
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: DNA polymerase X family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- monomeric PubMed
Database entries
- Structure:
- UniProt: P94544
- KEGG entry: [2]
- E.C. number: 2.7.7.7
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Margarita Salas, Madrid, Spain link
Your additional remarks
References
Benito Baños, Laurentino Villar, Margarita Salas, Miguel de Vega
Intrinsic apurinic/apyrimidinic (AP) endonuclease activity enables Bacillus subtilis DNA polymerase X to recognize, incise, and further repair abasic sites.
Proc Natl Acad Sci U S A: 2010, 107(45);19219-24
[PubMed:20974932]
[WorldCat.org]
[DOI]
(I p)
Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Characterization of a Bacillus subtilis 64-kDa DNA polymerase X potentially involved in DNA repair.
J Mol Biol: 2008, 384(5);1019-28
[PubMed:18938175]
[WorldCat.org]
[DOI]
(I p)
Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase.
Nucleic Acids Res: 2008, 36(18);5736-49
[PubMed:18776221]
[WorldCat.org]
[DOI]
(I p)
