Difference between revisions of "AtpD"

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* '''Description:''' ATP synthase (subunit beta) <br/><br/>
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* '''Description:''' [[ATP synthase]], part of the F1 complex (subunit beta) <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || ATP synthase (subunit beta))
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|style="background:#ABCDEF;" align="center"| '''Product''' || [[ATP synthase]] (subunit beta))
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || ATP synthesis  
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|style="background:#ABCDEF;" align="center"|'''Function''' || [[ATP synthesis]]
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU36810 atpD]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU36810 atpD]
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/AtpD AtpD]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 51 kDa, 4.611   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 51 kDa, 4.611   
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<br/><br/><br/><br/>
 
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** [[AtpB|A]](1)-[[AtpF|B]](2)-[[AtpE|C]](12) - [[AtpA|alpha]](3)-[[AtpD|beta]](3)-[[AtpG|gamma]]-[[AtpH|delta]]-[[AtpC|epsilon]]
  
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* '''[[Localization]]:''' cell membrane (according to Swiss-Prot),  membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]  
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* '''[[Localization]]:'''  
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** membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]  
 +
** peripheral via theF0 complex
  
 
=== Database entries ===
 
=== Database entries ===
  
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* '''Structure:'''
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* '''Structure:''' [http://www.rcsb.org/pdb/101/motm.do?momID=72&evtc=Suggest&evta=Moleculeof%20the%20Month&evtl=OtherOptions see here an overview on ATPase structure]
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37809 P37809]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37809 P37809]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=atpD_3781491_3782912_-1 atpD] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=atpD_3781491_3782912_-1 atpD] {{PubMed|22383849}}
  
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* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
−
 
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== Reviews ==
 +
<pubmed> 23356252 23341301, 23267178 22822068 21524994 19489730 17208001 16730323 </pubmed>
 +
== Original publications ==
 
<pubmed>7961438,,16493705 18763711, </pubmed>
 
<pubmed>7961438,,16493705 18763711, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:00, 11 August 2013

  • 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

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:
  • Domains:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s):
  • 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:

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

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