AddB

• Description: ATP-dependent deoxyribonuclease (subunit B)
  
  

Gene name	addB
Synonyms
Essential	no
Product	ATP-dependent deoxyribonuclease (subunit B))
Function	DNA repair and recombination
MW, pI	134 kDa, 5.39
Gene length, protein length	3498 bp, 1166 aa
Immediate neighbours	yhjR, addA
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: BSU10620

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: 1Y26 (the riboswitch in complex with adenine)

• UniProt: P23477

• 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)