addB [2017-8-11 16:0:3]

ATP-dependent deoxyribonuclease (subunit B), required for efficient survival and replication restart after replication-transcription conflicts

locus: BSU10620

pI: 5.39

mw: 134.41 kDa

protein length: 1166 aa

gene length: 3498 bp

function: DNA repair/ recombination

product: ATP-dependent deoxyribonuclease (subunit B))

essential: no

synonyms

Genomic Context

categories

• [category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.5|DNA repair/ recombination]
• [category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.5|DNA repair/ recombination] → [category|SW 3.1.5.6|Other proteins]
• [category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.7|Genetic competence]
• [category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.3|Genetic competence]

Gene

Coordinates: 1,136,320 → 1,139,820

Phenotypes of a mutant

• ''[gene|80E6F156764FF30300D034EE6FB44F2DB8338AF3|recO] [gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB]'' double mutants are extremely sensitive against DNA damaging agents [Pubmed|26001966]

The protein

Catalyzed reaction/ biological activity

• the enzyme is functional as a heterodimer of the [protein|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|AddA] and [protein|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|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 [protein|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|AddA] subunit [Pubmed|21071401]
• the [protein|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|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|21071401]

Protein family

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

Structure

• [PDB|3U4Q] (the [protein|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|AddA]-[protein|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|AddB]-DNA complex) [Pubmed|22307084]

Expression and Regulation

Operons

• genes: [gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB]-[gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|4D89BFFB1073407A7A1762AFD18B49F3414D6787|sbcD]-[gene|ED825D5B3290BA8F9C92477B1FCC433ADB3C8449|sbcC]-[gene|74E2AB77354355549D14152D3566C9B953A4CB31|hlpB]
  description: [Pubmed|22383849]

  sigma factors

  • [protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|7746142], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]

  regulatory mechanism

  • [protein|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK]: activation, in [regulon|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|ComK regulon]

  regulation

  • positive control by [protein|search|ComK] [Pubmed|7746142]

Biological materials

Mutant

• GP1106 ([gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB], spc), available in [SW|Jörg Stülke]'s lab

Labs working on this gene/protein

• [SW|Mark Dillingham], Bristol, U.K. ([http://www.bris.ac.uk/biochemistry/research/md.html homepage])

References

Reviews

• 23202527,20116346,22933559,19542287,25486468

Original publications

• 21809208,8387145,15610857,7746142,19129187,1646786,10756102,9781875,17570399,20350930,22307084,22383849,21071401,23056615,24682829,24670664,8752329,25939832,26001966,8510642