Difference between revisions of "AtpD"

From SubtiWiki
Jump to: navigation, search
Line 124: Line 124:
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 10748 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 10748 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4258 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6323 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:33, 17 April 2014

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

Gene name atpD
Synonyms
Essential no
Product ATP synthase (subunit beta))
Function ATP synthesis
Gene expression levels in SubtiExpress: atpD
Interactions involving this protein in SubtInteract: AtpD
MW, pI 51 kDa, 4.611
Gene length, protein length 1419 bp, 473 aa
Immediate neighbours atpC, atpG
Sequences Protein DNA DNA_with_flanks
Genetic context
AtpD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AtpD 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: BSU36810

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), ATP synthesis 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): 10748 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4258 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6323 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