PolX

• Description: DNA polymerase X, involved in DNA repair
  
  

Gene name	polX
Synonyms	yshC
Essential	no
Product	DNA polymerase X
Function	DNA repair
Gene expression levels in SubtiExpress: polX
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
Expression at a glance   PubMed

Categories containing this gene/protein

DNA repair/ recombination

The gene

Basic information

• Locus tag: BSU28590

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • template-dependent DNA polymerase, fills single nucleotide gaps PubMed
  • has intrinsic 3'-5' exonuclease activity for resecting unannealed 3'-termini in gapped DNA substrates PubMed
  • has intrinsic apurinic/apyrimidinic (AP) endonuclease activity PubMed

• 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

• Localization:

Database entries

• Structure:

• UniProt: P94544

• KEGG entry: [2]

• E.C. number: 2.7.7.7

Expression and regulation

• Operon:

• Expression browser: polX PubMed

• 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

Margarita Salas, Madrid, Spain link

References

Benito Baños, Laurentino Villar, Margarita Salas, Miguel de Vega
DNA stabilization at the Bacillus subtilis PolX core--a binding model to coordinate polymerase, AP-endonuclease and 3'-5' exonuclease activities.
Nucleic Acids Res: 2012, 40(19);9750-62
[PubMed:22844091] [WorldCat.org] [DOI] (I p)

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)