Difference between revisions of "Spo0E"
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU13640 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
Line 80: | Line 80: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P05043 P05043] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P05043 P05043] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13640] |
* '''E.C. number:''' | * '''E.C. number:''' |
Revision as of 14:16, 3 June 2009
- Description: Spo0A-P phosphatase
Gene name | spo0E |
Synonyms | |
Essential | no |
Product | Spo0A-P phosphatase |
Function | initiation of sporulation |
MW, pI | 9 kDa, 6.483 |
Gene length, protein length | 255 bp, 85 aa |
Immediate neighbours | ykvA, eag |
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: BSU13640
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: spo0E family (according to Swiss-Prot)
- Paralogous protein(s): YnzD
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P05043
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information: Spo0E is degraded by FtsH
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Tony Wilkinson, York University, U.K. homepage
Your additional remarks
References
Ai Thi Thuy Le, Wolfgang Schumann
The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease.
Microbiology (Reading): 2009, 155(Pt 4);1122-1132
[PubMed:19332814]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed