Difference between revisions of "AtpD"
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 10748 {{PubMed|24696501}} | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 10748 {{PubMed|24696501}} | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 {{PubMed|24696501}} | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4258 {{PubMed|21395229}} | ||
+ | |||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6323 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
Revision as of 13:33, 17 April 2014
- 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 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: BSU36810
Phenotypes of a mutant
Database entries
- BsubCyc: BSU36810
- 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:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Effectors of protein activity:
- Localization:
- membrane PubMed
- peripheral via theF0 complex
Database entries
- BsubCyc: BSU36810
- Structure: see here an overview on ATPase structure
- UniProt: P37809
- 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
- number of protein molecules per cell (minimal medium with glucose and ammonium): 10748 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 50616 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4258 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6323 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
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)
Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[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)