Difference between revisions of "DnaG"
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* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
− | * '''Effectors of protein activity:''' | + | * '''Effectors of protein activity:''' the enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ {{PubMed|17350574}} |
* '''Interactions:''' | * '''Interactions:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
− | ** enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ | + | ** enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ {{PubMed|17350574}} |
=Biological materials = | =Biological materials = |
Revision as of 14:41, 9 July 2009
- Description: DNA primase
Gene name | dnaG |
Synonyms | dnaE |
Essential | yes PubMed |
Product | DNA primase |
Function | DNA replication |
MW, pI | 68 kDa, 6.706 |
Gene length, protein length | 1809 bp, 603 aa |
Immediate neighbours | antE, yqxD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU25210
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:
- Protein family: DNA primase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: the enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed
- Interactions:
- Localization: Cytoplasm (Homogeneous) PubMed
Database entries
- Structure: 1D0Q (zinc binding domain, Geobacillus stearothermophilus), 1Z8S (DnaB binding domain, AA 452-597, Geobacillus stearothermophilus)
- Swiss prot entry: P05096
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Additional information:
- enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Kiran Chintakayala, Cristina Machón, Anna Haroniti, Marilyn A Larson, Steven H Hinrichs, Mark A Griep, Panos Soultanas
Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.
Mol Microbiol: 2009, 72(2);537-49
[PubMed:19415803]
[WorldCat.org]
[DOI]
(I p)
Jue D Wang, Glenn M Sanders, Alan D Grossman
Nutritional control of elongation of DNA replication by (p)ppGpp.
Cell: 2007, 128(5);865-75
[PubMed:17350574]
[WorldCat.org]
[DOI]
(P p)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
L F Wang, C W Price, R H Doi
Bacillus subtilis dnaE encodes a protein homologous to DNA primase of Escherichia coli.
J Biol Chem: 1985, 260(6);3368-72
[PubMed:3919021]
[WorldCat.org]
(P p)