Difference between revisions of "PycA"

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(Expression and regulation)
(References)
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[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:08, 19 January 2010

  • Description: pyruvate carboxylase

Gene name pycA
Synonyms ylaP
Essential no
Product pyruvate carboxylase
Function replenishment of the oxaloacetate pool
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 127 kDa, 5.407
Gene length, protein length 3444 bp, 1148 aa
Immediate neighbours ftsW, ctaA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PycA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU14860

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): biotin
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane associated PubMed

Database entries

  • Structure: 3BG5 (S. aureus)
  • KEGG entry: [3]
  • E.C. number: 6.4.1.1

Additional information

PycA binds to StrepTactin, and may be co-purified when purifying Strep-tagged proteins by SPINE.

PycA is subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)