Difference between revisions of "AtpE"
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− | * '''Description:''' ATP synthase (subunit c) <br/><br/> | + | * '''Description:''' [[ATP synthase]], part of the Fo complex (subunit c) <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 | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || ATP synthase (subunit c) | + | |style="background:#ABCDEF;" align="center"| '''Product''' || [[ATP synthase]] (subunit c) |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || ATP synthesis | + | |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=BSU36860 atpE] | |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=BSU36860 atpE] | ||
+ | |- | ||
+ | |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/AtpE AtpE] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 6 kDa, 6.433 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 6 kDa, 6.433 | ||
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<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
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− | |||
− | |||
− | |||
<br/><br/> | <br/><br/> | ||
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* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
+ | ** [[AtpB|A]](1)-[[AtpF|B]](2)-[[AtpE|C]](12) - [[AtpA|alpha]](3)-[[AtpD|beta]](3)-[[AtpG|gamma]]-[[AtpH|delta]]-[[AtpC|epsilon]] | ||
− | * '''[[Localization]]:''' membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | + | * '''[[Localization]]:''' |
+ | ** membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''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/P37815 P37815] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37815 P37815] | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=atpE_3786620_3786832_-1 atpE] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=atpE_3786620_3786832_-1 atpE] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
− | + | == Reviews == | |
+ | <pubmed> 23356252 23341301, 23267178 22822068 21524994 19489730 17208001 16730323 </pubmed> | ||
+ | == Original publications == | ||
<pubmed>7961438,,18763711, </pubmed> | <pubmed>7961438,,18763711, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:00, 11 August 2013
- Description: ATP synthase, part of the Fo complex (subunit c)
Gene name | atpE |
Synonyms | |
Essential | no |
Product | ATP synthase (subunit c) |
Function | ATP synthesis |
Gene expression levels in SubtiExpress: atpE | |
Interactions involving this protein in SubtInteract: AtpE | |
MW, pI | 6 kDa, 6.433 |
Gene length, protein length | 210 bp, 70 aa |
Immediate neighbours | atpF, atpB |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
ATP synthesis, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU36860
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP synthesis see a video
- Protein family: ATPase C chain family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane PubMed
Database entries
- Structure: see here an overview on ATPase structure
- UniProt: P37815
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
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)
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)