Difference between revisions of "PpaC"
| Line 82: | Line 82: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P37487 P37487] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P37487 P37487] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU40550] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.6.1.1 3.6.1.1] | * '''E.C. number:''' [http://www.expasy.org/enzyme/3.6.1.1 3.6.1.1] | ||
Revision as of 03:48, 25 June 2009
- Description: inorganic pyrophosphatase
| Gene name | ppaC |
| Synonyms | yybQ |
| Essential | yes PubMed |
| Product | inorganic pyrophosphatase |
| Function | recovery of phosphate ions from pyrophosphate |
| MW, pI | 33 kDa, 4.513 |
| Gene length, protein length | 927 bp, 309 aa |
| Immediate neighbours | yybR, yybP |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU40550
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Diphosphate + H2O = 2 phosphate (according to Swiss-Prot)
- Protein family: PPase class C family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: S-cysteinylation after diamide stress (C158) PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Swiss prot entry: P37487
- KEGG entry: [3]
- E.C. number: 3.6.1.1
Additional information
Expression and regulation
- Operon:
- 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
Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193]
[WorldCat.org]
[DOI]
(P p)
Igor P Fabrichniy, Lari Lehtiö, Anu Salminen, Anton B Zyryanov, Alexander A Baykov, Reijo Lahti, Adrian Goldman
Structural studies of metal ions in family II pyrophosphatases: the requirement for a Janus ion.
Biochemistry: 2004, 43(45);14403-11
[PubMed:15533045]
[WorldCat.org]
[DOI]
(P p)
