Difference between revisions of "DnaA"
Line 1: | Line 1: | ||
− | * '''Description:''' replication initiation protein <br/><br/> | + | * '''Description:''' AAA+ ATPase, replication initiation protein <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 35: | Line 35: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | |||
− | |||
− | |||
− | |||
<br/><br/> | <br/><br/> | ||
Line 72: | Line 68: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase [[DnaC]] | ||
* '''Protein family:''' dnaA family (according to Swiss-Prot) | * '''Protein family:''' dnaA family (according to Swiss-Prot) | ||
Line 91: | Line 88: | ||
** [[YabA]] inhibits co-operative binding of DnaA to the ''oriC'' DNA {{PubMed|21895792}} | ** [[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 [[Soj]] with the AAA+ domain of DnaA {{PubMed|22286949}} | ** DnaA helix formation (and thus replication initiation) is inhibited by the interaction of [[Soj]] with the AAA+ domain of DnaA {{PubMed|22286949}} | ||
+ | ** interaction with [[DnaD]] inhibits the ability of [[DnaA]] to cooperatively bind to DNA {{PubMed|22821970}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
Line 96: | Line 94: | ||
** [[Soj]]-[[DnaA]] {{PubMed|22286949}} | ** [[Soj]]-[[DnaA]] {{PubMed|22286949}} | ||
** [[DnaA]]-[[YabA]], [[DnaA]]-[[YabA]]-[[DnaN]] {{PubMed|12060778}} | ** [[DnaA]]-[[YabA]], [[DnaA]]-[[YabA]]-[[DnaN]] {{PubMed|12060778}} | ||
− | ** [[DnaA]]-[[DnaD]] | + | ** [[DnaA]]-[[DnaD]] {{PubMed|22821970,11222620}} |
** [[SirA]]-[[DnaA]] {{PubMed|19682252,21239581}} | ** [[SirA]]-[[DnaA]] {{PubMed|19682252,21239581}} | ||
** [[YqaH]]-[[DnaA]] {{PubMed|12060778}} | ** [[YqaH]]-[[DnaA]] {{PubMed|12060778}} | ||
Line 146: | Line 144: | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
− | [[Philippe Noirot]], Jouy-en-Josas, France [http://locus.jouy.inra.fr/cms/index.php?id=18 homepage] | + | * [[Philippe Noirot]], Jouy-en-Josas, France [http://locus.jouy.inra.fr/cms/index.php?id=18 homepage] |
− | + | * [[Peter Graumann]], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage] | |
− | [[Peter Graumann]], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage] | + | * [[Alan Grossman]], MIT, Cambridge, MA, USA |
− | |||
− | [[Alan Grossman]], MIT, Cambridge, MA, USA | ||
=Your additional remarks= | =Your additional remarks= | ||
Line 162: | Line 158: | ||
==Original publications== | ==Original publications== | ||
'''Additional publications:''' {{PubMed|22396664,21911367}} | '''Additional publications:''' {{PubMed|22396664,21911367}} | ||
− | <pubmed>18854156,19011033, 11222620,14651647,17140409 10844689 ,11222620 12060778 16461910 2987848 2168872 11207367, 19737352 19081080 17932079 19968790 19682252 20511500 21097613 21239581 21895792 22286949</pubmed> | + | <pubmed>18854156,19011033, 11222620,14651647,17140409 10844689 ,11222620 12060778 16461910 2987848 2168872 11207367, 19737352 19081080 17932079 19968790 19682252 20511500 21097613 21239581 21895792 22286949 22821970</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:42, 24 July 2012
- Description: AAA+ ATPase, replication initiation protein
Gene name | dnaA |
Synonyms | dnaH, dnaJ, dnaK |
Essential | yes PubMed |
Product | replication initiation protein |
Function | DNA replication |
Interactions involving this protein in SubtInteract: DnaA | |
MW, pI | 50 kDa, 6.035 |
Gene length, protein length | 1338 bp, 446 aa |
Immediate neighbours | rpmH, dnaN |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
DNA replication, essential genes
This gene is a member of the following regulons
The DnaA regulon
The gene
Basic information
- Locus tag: BSU00010
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase DnaC
- Protein family: dnaA family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: AAA+ domain
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- SirA displaces DnaA from the replication origin PubMed
- YabA inhibits co-operative binding of DnaA to the oriC DNA PubMed
- DnaA helix formation (and thus replication initiation) is inhibited by the interaction of Soj with the AAA+ domain of DnaA PubMed
- interaction with DnaD inhibits the ability of DnaA to cooperatively bind to DNA PubMed
- Localization: throughout the cytoplasm PubMed
Database entries
- Structure:
- UniProt: P05648
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Philippe Noirot, Jouy-en-Josas, France homepage
- Peter Graumann, Freiburg University, Germany homepage
- Alan Grossman, MIT, Cambridge, MA, USA
Your additional remarks
References
Reviews
Geoffrey S Briggs, Wiep Klaas Smits, Panos Soultanas
Chromosomal replication initiation machinery of low-G+C-content Firmicutes.
J Bacteriol: 2012, 194(19);5162-70
[PubMed:22797751]
[WorldCat.org]
[DOI]
(I p)
An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476]
[WorldCat.org]
[DOI]
(I p)
Alan C Leonard, Julia E Grimwade
Regulation of DnaA assembly and activity: taking directions from the genome.
Annu Rev Microbiol: 2011, 65;19-35
[PubMed:21639790]
[WorldCat.org]
[DOI]
(I p)
Alan C Leonard, Julia E Grimwade
Regulating DnaA complex assembly: it is time to fill the gaps.
Curr Opin Microbiol: 2010, 13(6);766-72
[PubMed:21035377]
[WorldCat.org]
[DOI]
(I p)
Tsutomu Katayama, Shogo Ozaki, Kenji Keyamura, Kazuyuki Fujimitsu
Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC.
Nat Rev Microbiol: 2010, 8(3);163-70
[PubMed:20157337]
[WorldCat.org]
[DOI]
(I p)
The DnaA regulon
Alexi I Goranov, Luba Katz, Adam M Breier, Christopher B Burge, Alan D Grossman
A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA.
Proc Natl Acad Sci U S A: 2005, 102(36);12932-7
[PubMed:16120674]
[WorldCat.org]
[DOI]
(P p)
Original publications
Additional publications: PubMed