Difference between revisions of "FtsH"

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Revision as of 12:19, 16 May 2013

  • 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 DNA_with_flanks
Genetic context
FtsH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FtsH expression.png















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]

Additional information

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:

Database entries

  • Structure: 1LV7 (from E. coli, 64% identity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: induced by heat shock (class III)
  • 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

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)