Difference between revisions of "AtpF"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36850&redirect=T BSU36850] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/atp.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/atp.html] | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36850&redirect=T BSU36850] | ||
* '''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] | * '''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] |
Revision as of 15:02, 2 April 2014
- Description: ATP synthase, part of the Fo complex (subunit b)
Gene name | atpF |
Synonyms | |
Essential | no |
Product | ATP synthase (subunit b)) |
Function | ATP synthesis |
Gene expression levels in SubtiExpress: atpF | |
Interactions involving this protein in SubtInteract: AtpF | |
MW, pI | 19 kDa, 4.921 |
Gene length, protein length | 510 bp, 170 aa |
Immediate neighbours | atpH, atpE |
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: BSU36850
Phenotypes of a mutant
Database entries
- BsubCyc: BSU36850
- 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 B 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
- BsubCyc: BSU36850
- Structure: see here an overview on ATPase structure
- UniProt: P37814
- 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