PpaC

• 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	hypR, yybP
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

phosphate metabolism, essential genes

The gene

Basic information

• Locus tag: BSU40550

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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
  • S-bacillithiolation upon hypochlorite stress on Cys-158 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2HAW (complex with substrate analogue p-nitrophosphate), 1WPM

• UniProt: P37487

• KEGG entry: [3]

• E.C. number: 3.6.1.1

Expression and regulation

• Operon: ppaC (according to DBTBS)

• Expression browser: ppaC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)