AtpA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU36830

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • A(1)-B(2)-C(12) - alpha(3)-beta(3)-gamma-delta-epsilon

• Localization:
  • membrane PubMed
  • peripheral via theF0 complex

Database entries

• BsubCyc: BSU36830

• Structure: see here an overview on ATPase structure

• UniProt: P37808

• KEGG entry: [3]

• E.C. number: 3.6.3.14

Expression and regulation

• Operon: atpI-atpB-atpE-atpF-atpH-atpA-atpG-atpD-atpC PubMed

• Expression browser: atpA PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)