addA

addA
168

ATP-dependent deoxyribonuclease (subunit A), required for efficient survival and replication restart after replication-transcription conflicts, responsible for end resection during dsDNA break repair

locus
BSU_10630
Molecular weight
140.85 kDa
pI
5.13
Protein length
Gene length
function
DNA repair/ recombination
product
ATP-dependent deoxyribonuclease (subunit A))
essential
no
synonyms
addA, recE5

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1074 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,139,807  1,143,505
Phenotypes of a mutant
reduced survival after mitomycin treatment [pubmed|34339298]
[gene|80E6F156764FF30300D034EE6FB44F2DB8338AF3|recO] [gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB] double mutants are extremely sensitive against DNA damaging agents [Pubmed|26001966]
reduced survival after [category|SW.3.1.1|DNA replication] arrest imposed by inhibition of [protein|FB97DF0C147FB29944F60214CB9BC1803861DAA0|polC] activity [pubmed|36574412]
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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]
ATP + H2O --> ADP + H+ + phosphate (according to UniProt)
Protein family
[wiki|helicase family] (according to UniProt)
[wiki|Domains]
[wiki|UvrD-like helicase ATP-binding domain](aa 9-481) (according to UniProt)
[wiki|UvrD-like helicase C-terminal domain] (aa 508-798) (according to UniProt)
Structure
[PDB|3U4Q] (the [protein|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[protein|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB]-DNA complex) [Pubmed|22307084]
[AF|P23478]
Expression and Regulation
Operons
genes
[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB]-[gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|4D89BFFB1073407A7A1762AFD18B49F3414D6787|sbcD]-[gene|ED825D5B3290BA8F9C92477B1FCC433ADB3C8449|sbcC]-[gene|74E2AB77354355549D14152D3566C9B953A4CB31|hlpB]
description
[Pubmed|22383849]
regulation
positive control by [protein|search|ComK] [Pubmed|7746142]
regulatory mechanism
[protein|08CFA2C72931A75532D4289BC1D18A826DE9F9CA|comK]: activation, in [regulon|protein:08CFA2C72931A75532D4289BC1D18A826DE9F9CA|comK regulon]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA]: sigma factor, [Pubmed|7746142], in [regulon|protein:360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA regulon]
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[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB]→[gene|74E2AB77354355549D14152D3566C9B953A4CB31|hlpB]

2024-03-11 09:07:21

ghost

109

045c7bb396e5f5521fcc2041130afbaac29b0bd8

E5051999C31DBE142375FC331C2F21A76C29910D

Biological materials
Mutant
GP1106 ([gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]-[gene|55A1EF8A10CB398CCD3FDD06D9483FE0DCE31C64|addB], spc), available in [wiki|Jörg Stülke]'s lab [pubmed|22178973]
BKE10630 ([gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]::erm  trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKE10630 BGSC],  [Pubmed|28189581], upstream reverse: _UP1_ATCTGTCCATGTGCTGTCTG,  downstream forward: _UP4_TAGCGAGATCCATAAGCTCC
BKK10630 ([gene|49E8BFEC1CAB77DD91E0ED0791EBD480E4871239|addA]::kan  trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKK10630 BGSC],  [Pubmed|28189581], upstream reverse: _UP1_ATCTGTCCATGTGCTGTCTG,  downstream forward: _UP4_TAGCGAGATCCATAAGCTCC
labs
[wiki|Mark Dillingham], Bristol, U.K. ([http://www.bris.ac.uk/biochemistry/research/md.html homepage])
References
Reviews
23202527,20116346,22933559,19542287,25486468,32286623,36030574
Original Publications
8387145,15610857,7746142,19129187,15009890,10756102,9781875,16632468,17570399,20350930,21809208,21821766,22307084,24682829,24670664,22383849,21071401,8752329,8752323,25939832,26001966,8510642,33085588,34339298,36574412

49E8BFEC1CAB77DD91E0ED0791EBD480E4871239

Page visits: 4641

Time of last update: 2024-03-29 14:17:03

Author of last update: Jstuelk