Difference between revisions of "PpaC"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[phosphate metabolism]]}}, | {{SubtiWiki category|[[phosphate metabolism]]}}, | ||
| − | {{SubtiWiki category|[[essential genes]]}} | + | {{SubtiWiki category|[[essential genes]]}}, |
| + | [[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=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
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** Cys158 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species {{PubMed|21749987}} {{PubMed|21749987}} | ** Cys158 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species {{PubMed|21749987}} {{PubMed|21749987}} | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ppaC_4168204_4169133_1 ppaC] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ppaC_4168204_4169133_1 ppaC] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed>22938038,21749987,15533045,17611193,9845334 9782505 11342544, 9633597 21749987</pubmed> | + | <pubmed>22938038,21749987,15533045,17611193,9845334 9782505 11342544, 9633597 21749987 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:16, 5 March 2014
- Description: inorganic pyrophosphatase
| Gene name | ppaC |
| Synonyms | yybQ |
| Essential | yes PubMed |
| Product | inorganic pyrophosphatase |
| Function | recovery of phosphate ions from pyrophosphate |
| Gene expression levels in SubtiExpress: ppaC | |
| MW, pI | 33 kDa, 4.513 |
| Gene length, protein length | 927 bp, 309 aa |
| Immediate neighbours | hypR, yybP |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
| Expression at a glance PubMed 500px | |
Contents
Categories containing this gene/protein
phosphate metabolism, essential genes, most abundant proteins
This gene is a member of the following regulons
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:
- Modification:
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P37487
- KEGG entry: [3]
- E.C. number: 3.6.1.1
Additional information
Expression and regulation
- Operon: ppaC (according to DBTBS)
- 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
Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038]
[WorldCat.org]
[DOI]
(I p)
Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987]
[WorldCat.org]
[DOI]
(I p)
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)
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)
A N Parfenyev, A Salminen, P Halonen, A Hachimori, A A Baykov, R Lahti
Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans.
J Biol Chem: 2001, 276(27);24511-8
[PubMed:11342544]
[WorldCat.org]
[DOI]
(P p)
T Shintani, T Uchiumi, T Yonezawa, A Salminen, A A Baykov, R Lahti, A Hachimori
Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes.
FEBS Lett: 1998, 439(3);263-6
[PubMed:9845334]
[WorldCat.org]
[DOI]
(P p)
Tom W Young, Nicholas J Kuhn, Albert Wadeson, Simon Ward, Dan Burges, G Dunstan Cooke
Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic pyrophosphatase with distinctive properties: the first of a new class of soluble pyrophosphatase?
Microbiology (Reading): 1998, 144 ( Pt 9);2563-2571
[PubMed:9782505]
[WorldCat.org]
[DOI]
(P p)
N J Kuhn, S Ward
Purification, properties, and multiple forms of a manganese-activated inorganic pyrophosphatase from Bacillus subtilis.
Arch Biochem Biophys: 1998, 354(1);47-56
[PubMed:9633597]
[WorldCat.org]
[DOI]
(P p)
