AddA

• Description: ATP-dependent deoxyribonuclease (subunit A)
  
  

Gene name	addA
Synonyms	recE5
Essential	no
Product	ATP-dependent deoxyribonuclease (subunit A))
Function	DNA repair and recombination
MW, pI	140 kDa, 5.127
Gene length, protein length	3696 bp, 1232 aa
Immediate neighbours	addB, sbcD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU10630

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3'→5' polarity located in the AddA subunit PubMed
  • the AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences PubMed

• Protein family: uvrD-like helicase C-terminal domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: AddA-AddB PubMed

• Localization:

Database entries

• Structure:

• UniProt: P23478

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: addB-addA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • positive control by ComK PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP1106 (addAB, spc), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Joseph T P Yeeles, Mark S Dillingham
The processing of double-stranded DNA breaks for recombinational repair by helicase-nuclease complexes.
DNA Repair (Amst): 2010, 9(3);276-85
[PubMed:20116346] [WorldCat.org] [DOI] (I p)

Original publications

Additional publications: PubMed