Difference between revisions of "AtpA"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 6807 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 41984 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:53, 17 April 2014

  • Description: ATP synthase, part of the F1 complex (subunit alpha)

Gene name atpA
Synonyms
Essential no
Product ATP synthase (subunit alpha))
Function ATP synthesis
Gene expression levels in SubtiExpress: atpA
Interactions involving this protein in SubtInteract: AtpA
MW, pI 54 kDa, 5.04
Gene length, protein length 1506 bp, 502 aa
Immediate neighbours atpG, atpH
Sequences Protein DNA DNA_with_flanks
Genetic context
AtpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AtpA expression.png















Categories containing this gene/protein

ATP synthesis, membrane proteins, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU36830

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + H2O + H+(In) = ADP + phosphate + H+(Out) (according to Swiss-Prot) see a video
  • Protein family: ATPase alpha/beta chains family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 6807 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 41984 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

John E Walker
The ATP synthase: the understood, the uncertain and the unknown.
Biochem Soc Trans: 2013, 41(1);1-16
[PubMed:23356252] [WorldCat.org] [DOI] (I p)

Ryota Iino, Hiroyuki Noji
Operation mechanism of F(o) F(1)-adenosine triphosphate synthase revealed by its structure and dynamics.
IUBMB Life: 2013, 65(3);238-46
[PubMed:23341301] [WorldCat.org] [DOI] (I p)

Hendrik Sielaff, Michael Börsch
Twisting and subunit rotation in single F(O)(F1)-ATP synthase.
Philos Trans R Soc Lond B Biol Sci: 2013, 368(1611);20120024
[PubMed:23267178] [WorldCat.org] [DOI] (I e)

Alan E Senior
Two ATPases.
J Biol Chem: 2012, 287(36);30049-62
[PubMed:22822068] [WorldCat.org] [DOI] (I p)

Daichi Okuno, Ryota Iino, Hiroyuki Noji
Rotation and structure of FoF1-ATP synthase.
J Biochem: 2011, 149(6);655-64
[PubMed:21524994] [WorldCat.org] [DOI] (I p)

Christoph von Ballmoos, Alexander Wiedenmann, Peter Dimroth
Essentials for ATP synthesis by F1F0 ATP synthases.
Annu Rev Biochem: 2009, 78;649-72
[PubMed:19489730] [WorldCat.org] [DOI] (I p)

Joachim Weber
ATP synthase--the structure of the stator stalk.
Trends Biochem Sci: 2007, 32(2);53-6
[PubMed:17208001] [WorldCat.org] [DOI] (P p)

Joachim Weber
ATP synthase: subunit-subunit interactions in the stator stalk.
Biochim Biophys Acta: 2006, 1757(9-10);1162-70
[PubMed:16730323] [WorldCat.org] [DOI] (P p)

Original publications

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)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

M Santana, M S Ionescu, A Vertes, R Longin, F Kunst, A Danchin, P Glaser
Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants.
J Bacteriol: 1994, 176(22);6802-11
[PubMed:7961438] [WorldCat.org] [DOI] (P p)