Difference between revisions of "DnaB"
| Line 35: | Line 35: | ||
=== Basic information === | === Basic information === | ||
| − | * '''Locus tag:''' | + | * '''Locus tag:''' BSU28990 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| Line 82: | Line 82: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P07908 P07908] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P07908 P07908] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU28990] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
Revision as of 13:43, 3 June 2009
- Description: initiation of chromosome replication/ membrane attachment protein
| Gene name | dnaB |
| Synonyms | |
| Essential | yes PubMed |
| Product | initiation of chromosome replication/ membrane attachment protein |
| Function | DNA replication |
| MW, pI | 54 kDa, 5.278 |
| Gene length, protein length | 1416 bp, 472 aa |
| Immediate neighbours | dnaI, ytcG |
| 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: BSU28990
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:
- 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: P07908
- KEGG entry: [2]
- E.C. number:
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)
Y Imai, N Ogasawara, D Ishigo-Oka, R Kadoya, T Daito, S Moriya
Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids.
Mol Microbiol: 2000, 36(5);1037-48
[PubMed:10844689]
[WorldCat.org]
[DOI]
(P p)
