Difference between revisions of "AtpH"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36840&redirect=T BSU36840] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/atp.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/atp.html] | ||
Line 97: | Line 98: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU36840&redirect=T BSU36840] | ||
* '''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 F1 complex (subunit delta)
Gene name | atpH |
Synonyms | |
Essential | no |
Product | ATP synthase (subunit delta)) |
Function | ATP synthesis |
Gene expression levels in SubtiExpress: atpH | |
Interactions involving this protein in SubtInteract: AtpH | |
MW, pI | 19 kDa, 9.572 |
Gene length, protein length | 543 bp, 181 aa |
Immediate neighbours | atpA, atpF |
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, phosphoproteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU36840
Phenotypes of a mutant
Database entries
- BsubCyc: BSU36840
- 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 delta chain family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-159 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane (Heterogeneous) PubMed
- peripheral via theF0 complex
Database entries
- BsubCyc: BSU36840
- Structure: see here an overview on ATPase structure
- UniProt: P37811
- 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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P 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)