FtsH

• Description: ATP-dependent metalloprotease
  
  

Gene name	ftsH
Synonyms
Essential	no
Product	ATP-dependent metalloprotease
Function	cell division, sporulation initiation
Gene expression levels in SubtiExpress: ftsH
Interactions involving this protein in SubtInteract: FtsH
Metabolic function and regulation of this protein in SubtiPathways: Phosphorelay, Stress
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
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, cell envelope stress proteins (controlled by SigM, V, W, X, Y), heat shock proteins, biofilm formation, membrane proteins

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

• Locus tag: BSU00690

Phenotypes of a mutant

• defective in biofilm formation PubMed
• strongly reduced sporulation frequency PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: degrades Spo0E and Spo0M, resulting in reduced sporulation frequency in a ftsH mutant PubMed

• Protein family:

• Paralogous protein(s): YjoB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • SpoVM-FtsH PubMed
  • FloT-FtsH PubMed
  • FloA-FtsH PubMed
  • FtsH-Spo0E PubMed
  • FtsH-Spo0M PubMed

• Localization:
  • cell membrane PubMed
  • preferentially at the division septum PubMed
  • forms some foci in the membrane PubMed

Database entries

• Structure: 1LV7 (from E. coli, 64% identity) PubMed

• UniProt: P37476

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • ftsH PubMed
  • tilS-hprT-ftsH PubMed

• Expression browser: ftsH PubMed

• Sigma factor: SigA PubMed, SigM PubMed

• Regulation: induced by heat shock (class III)

• Regulatory mechanism:

• Additional information:
  • the mRNA is very stable (half-life > 15 min) PubMed
  • the FtsH levels are reduced in a floT floA double mutant PubMed

Biological materials

• Mutant:
  • 1A1061 ( ftsH::cat), PubMed, available at BGSC
  • 1A1060 ( ftsH::erm), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Additional reviews: PubMed

Original publications

Additional publications: PubMed

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)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

Matthias Kotschwar, Evita Harfst, Tanja Ohanjan, Wolfgang Schumann
Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains.
Curr Microbiol: 2004, 49(3);180-5
[PubMed:15386101] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

Stephan Zellmeier, Ulrich Zuber, Wolfgang Schumann, Thomas Wiegert
The absence of FtsH metalloprotease activity causes overexpression of the sigmaW-controlled pbpE gene, resulting in filamentous growth of Bacillus subtilis.
J Bacteriol: 2003, 185(3);973-82
[PubMed:12533473] [WorldCat.org] [DOI] (P p)

Szymon Krzywda, Andrzej M Brzozowski, Chandra Verma, Kiyonobu Karata, Teru Ogura, Anthony J Wilkinson
The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution.
Structure: 2002, 10(8);1073-83
[PubMed:12176385] [WorldCat.org] [DOI] (P p)

R S Prajapati, T Ogura, S M Cutting
Structural and functional studies on an FtsH inhibitor from Bacillus subtilis.
Biochim Biophys Acta: 2000, 1475(3);353-9
[PubMed:10913836] [WorldCat.org] [DOI] (P p)

W Wehrl, M Niederweis, W Schumann
The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation.
J Bacteriol: 2000, 182(13);3870-3
[PubMed:10851010] [WorldCat.org] [DOI] (P p)

W Schumann
FtsH--a single-chain charonin?
FEMS Microbiol Rev: 1999, 23(1);1-11
[PubMed:10077851] [WorldCat.org] [DOI] (P p)

M M Nakano, Y P Dailly, P Zuber, D P Clark
Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth.
J Bacteriol: 1997, 179(21);6749-55
[PubMed:9352926] [WorldCat.org] [DOI] (P p)

Elena Lysenko, Teru Ogura, Simon M Cutting
Characterization of the ftsH gene of Bacillus subtilis.
Microbiology (Reading): 1997, 143 ( Pt 3);971-978
[PubMed:9084181] [WorldCat.org] [DOI] (P p)

E Deuerling, A Mogk, C Richter, M Purucker, W Schumann
The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion.
Mol Microbiol: 1997, 23(5);921-33
[PubMed:9076729] [WorldCat.org] [DOI] (P p)

E Deuerling, B Paeslack, W Schumann
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift.
J Bacteriol: 1995, 177(14);4105-12
[PubMed:7608085] [WorldCat.org] [DOI] (P p)