Difference between revisions of "DnaB"
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|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | ||
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| − | |style="background:#ABCDEF;" align="center"| '''Essential''' || | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] |
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|style="background:#ABCDEF;" align="center"| '''Product''' || membrane attachment protein | |style="background:#ABCDEF;" align="center"| '''Product''' || membrane attachment protein | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| + | |||
| + | essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] | ||
=== Database entries === | === Database entries === | ||
Revision as of 16:01, 11 February 2009
- Description: write here
| Gene name | dnaB |
| Synonyms | |
| Essential | yes PubMed |
| Product | membrane attachment protein |
| Function | initiation of chromosome replication |
| MW, pI | 54 kDa, 5.278 |
| Gene length, protein length | 1416 bp, 472 aa |
| Immediate neighbours | |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
| |
Contents
The gene
Basic information
- Coordinates:
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: forms foci, close to oriC PubMed
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
- Haroniti et al. (2004) The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus.J. Mol. Biol. 336: 381-393. PubMed
- Imai et al. (2000) Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids. Mol. Microbiol. 36: 1037-1048. PubMed
