AAA ATPase, [category|SW 3.1.1|replication] initiation protein
function
[category|SW 3.1.1|DNA replication]
product
replication initiation protein
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.1|DNA replication][category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]Gene
Phenotypes of a mutant
essential [Pubmed|12682299]The protein
Catalyzed reaction/ biological activity
binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase [protein|5CF09E089AA70A32F640CE0D33D1F05312AAE24D|DnaC]Protein family
dnaA family (according to Swiss-Prot)[SW|Domains]
AAA + domainEffectors of protein activity
[protein|03595BF6DB8AE79604A720A5BD85C0DB781EE306|SirA] displaces [protein|6740108089F13116F200C15F35C2E7561E990FEB|DnaA] from the replication origin [Pubmed|19682252][protein|A039228A3805F4E7C5C2AE31C7DB0808562E88E3|YabA] inhibits co-operative binding of DnaA to the ''oriC'' DNA [Pubmed|21895792]DnaA helix formation (and thus replication initiation) is inhibited by the interaction of either [protein|5B3DB5A796ACA48390278E60478DFF13D0074A8D|ParA], [protein|A039228A3805F4E7C5C2AE31C7DB0808562E88E3|YabA] or [protein|83E05071DEC874248D3E96B8F3A093C65939B314|DnaN] with the AAA domain of DnaA [Pubmed|23909787,22286949]interaction with [protein|C9FEE07601AD28B2651EB881A1D9B34D5082237C|DnaD] inhibits the ability of [protein|6740108089F13116F200C15F35C2E7561E990FEB|DnaA] to cooperatively bind to DNA [Pubmed|22821970]DNA gyrase ([protein|B207C7328177924B16F1C606F667BEADF12CA069|GyrA]-[protein|AA42910B71348EFEA4165CFFCEF1E497897B9DDC|GyrB]) inhibits association of DnaA with [gene|search|oriC] [pubmed|29396913]Structure
[PDB|2Z4R] (from ''Thermotoga maritima '') [Pubmed|18216012][SW|Localization]
throughout the cytoplasm [Pubmed|10844689]co-localizes with the origin region and replication forks throughout the cell cycle [pubmed|28166228]Expression and Regulation
Operons
genes
[gene|6740108089F13116F200C15F35C2E7561E990FEB|dnaA]-[gene|83E05071DEC874248D3E96B8F3A093C65939B314|dnaN]
description
[Pubmed|2987848]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|2987848], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]regulatory mechanism
[protein|2C54FE2ADC82FF414D732018C90649D477A925AD|Spo0A]: repression, [Pubmed|14651647], in [regulon|2C54FE2ADC82FF414D732018C90649D477A925AD|Spo0A regulon]regulation
negatively controlled by [protein|search|DnaA] [Pubmed|2168872] and [SW|Spo0A] [Pubmed|14651647]additional information
term-seq has identified a potential novel regulatory RNA element including an intrinsic transcription terminator upstream of ''dnaA'' [Pubmed|27120414]view in new tablabs
[SW|Peter Graumann], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage][SW|Alan Grossman], MIT, Cambridge, MA, USA[SW|Heath Murray], Centre for Bacterial Cell Biology, Newcastle, UK [http://www.ncl.ac.uk/camb/staff/profile/heath.murray homepage]References
Reviews
20157337,21035377,21639790,22575476,22797751,26706151,28075389 The [SW|DnaA regulon]
Original publications
20511500,21097613,21239581,21895792,22286949,22821970,23909787,22396664,21911367,25041308,25340815,26020636,18854156,19011033,11222620,14651647,17140409,10844689,11222620,12060778,16461910,2987848,11207367,19737352,19081080,17932079,19968790,19682252,18216012,2168872,26615189,27120414,27489185,27902860,28166228,28752667,29396913,30285297,30534966