Difference between revisions of "DnaX"
| Line 37: | Line 37: | ||
=== Basic information === | === Basic information === | ||
| − | * '''Locus tag:''' | + | * '''Locus tag:''' BSU00190 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| Line 84: | Line 84: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P09122 P09122] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P09122 P09122] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU00190] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.7.7 2.7.7.7] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.7.7 2.7.7.7] | ||
Revision as of 13:44, 3 June 2009
- Description: DNA polymerase III (gamma and tau subunits)
| Gene name | dnaX |
| Synonyms | dnaH, dna-8132 |
| Essential | yes PubMed |
| Product | DNA polymerase III (gamma and tau subunits) |
| Function | DNA replication |
| MW, pI | 62 kDa, 5.488 |
| Gene length, protein length | 1689 bp, 563 aa |
| Immediate neighbours | scr, yaaK |
| 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: BSU00190
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- Swiss prot entry: P09122
- KEGG entry: [2]
- E.C. number: 2.7.7.7
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
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)
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)
Anna Haroniti, Christopher Anderson, Zara Doddridge, Laurence Gardiner, Clive J Roberts, Stephanie Allen, Panos Soultanas
The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus.
J Mol Biol: 2004, 336(2);381-93
[PubMed:14757052]
[WorldCat.org]
[DOI]
(P p)
A Haroniti, R Till, M C M Smith, P Soultanas
Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein.
Biochemistry: 2003, 42(37);10955-64
[PubMed:12974630]
[WorldCat.org]
[DOI]
(P p)
