Difference between revisions of "AtpA"

From SubtiWiki
Jump to: navigation, search
Line 42: Line 42:
 
{{SubtiWiki category|[[ATP synthesis]]}},
 
{{SubtiWiki category|[[ATP synthesis]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
{{SubtiWiki category|[[phosphoproteins]]}}
+
{{SubtiWiki category|[[phosphoproteins]]}},
 +
[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
Line 62: Line 63:
  
 
=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
Line 80: Line 78:
 
* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''[[Domains]]:'''  
  
 
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]  
 
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]  
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
Line 121: Line 119:
  
 
* '''Additional information:'''
 
* '''Additional information:'''
 +
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
Line 144: Line 143:
 
<pubmed> 23356252 23341301, 23267178 22822068 21524994 19489730 17208001 16730323 </pubmed>
 
<pubmed> 23356252 23341301, 23267178 22822068 21524994 19489730 17208001 16730323 </pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>7961438,,16493705 18763711, </pubmed>
+
<pubmed>7961438,15378759,16493705 18763711, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:16, 5 March 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:

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