PpaC

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  • 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
PpaC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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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:
    • S-cysteinylation after diamide stress (C158) PubMed
    • Cys158 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 2HAW (complex with substrate analogue p-nitrophosphate), 1WPM
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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): 4150 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 10163 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)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [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)