Difference between revisions of "AtpA"
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{{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]] = | ||
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=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
− | |||
=The protein= | =The protein= | ||
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* '''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] | ||
− | * ''' | + | * '''[[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 = | ||
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<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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
ATP synthesis, membrane proteins, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
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:
- Localization:
- membrane PubMed
- peripheral via theF0 complex
Database entries
- Structure: see here an overview on ATPase structure
- UniProt: P37808
- KEGG entry: [3]
- E.C. number: 3.6.3.14
Additional information
Expression and regulation
- 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:
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