Difference between revisions of "PpaC"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[hypR]]'', ''[[yybP]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[hypR]]'', ''[[yybP]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU40550 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU40550 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU40550 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU40550 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU40550 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU40550 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ppaC_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ppaC_context.gif]]

Revision as of 11:45, 14 May 2013

  • 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

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:
  • Domains:
  • Modification:
    • S-cysteinylation after diamide stress (C158) PubMed
    • Cys158 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Operon: ppaC (according to DBTBS)
  • Sigma factor:
  • 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

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)

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)

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