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
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, proteolysis, 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)