FtsH
- Description: ATP-dependent metalloprotease
Gene name | ftsH |
Synonyms | |
Essential | no |
Product | ATP-dependent metalloprotease |
Function | cell division, sporulation initiation |
MW, pI | 70 kDa, 5.841 |
Gene length, protein length | 1911 bp, 637 aa |
Immediate neighbours | hprT, coaX |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag:
Phenotypes of a mutant
strongly reduced sporulation frequency
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: degrades Spo0E, resulting in reduced sporulation frequency in a ftsH mutant
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot), membrane PubMed
Database entries
- Structure:
- Swiss prot entry: P37476
- KEGG entry: BSU00690
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation: induced by heat shock (class III)
- Regulatory mechanism:
- Additional information: the mRNA is very stable (half-life > 15 min) PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
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)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed