Difference between revisions of "PycA"

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(Biological materials)
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:'''
+
* '''Mutant:'''** GP793 (cat), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:10, 13 August 2013

  • Description: pyruvate carboxylase

Gene name pycA
Synonyms ylaP
Essential no
Product pyruvate carboxylase
Function replenishment of the oxaloacetate pool
Gene expression levels in SubtiExpress: pycA
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Biotin
MW, pI 127 kDa, 5.407
Gene length, protein length 3444 bp, 1148 aa
Immediate neighbours ftsW, ctaA
Sequences Protein DNA DNA_with_flanks
Genetic context
PycA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PycA expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

stringent response

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:

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:
    • subject to positive stringent control upon lysine starvation PubMed
  • Regulatory mechanism:
    • stringent response: due to presence of adenines at +1 and +2 positions of the transcript PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Expression vector:
    • pGP1289 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Sarawut Jitrapakdee, Martin St Maurice, Ivan Rayment, W Wallace Cleland, John C Wallace, Paul V Attwood
Structure, mechanism and regulation of pyruvate carboxylase.
Biochem. J.: 2008, 413(3);369-87
[PubMed:18613815] [WorldCat.org] [DOI] (I p)

Sarawut Jitrapakdee, John C Wallace
The biotin enzyme family: conserved structural motifs and domain rearrangements.
Curr. Protein Pept. Sci.: 2003, 4(3);217-29
[PubMed:12769720] [WorldCat.org] (P p)

S Jitrapakdee, J C Wallace
Structure, function and regulation of pyruvate carboxylase.
Biochem. J.: 1999, 340 ( Pt 1);1-16
[PubMed:10229653] [WorldCat.org] (P p)

J C Wallace, S Jitrapakdee, A Chapman-Smith
Pyruvate carboxylase.
Int. J. Biochem. Cell Biol.: 1998, 30(1);1-5
[PubMed:9597748] [WorldCat.org] (P p)

P V Attwood
The structure and the mechanism of action of pyruvate carboxylase.
Int. J. Biochem. Cell Biol.: 1995, 27(3);231-49
[PubMed:7780827] [WorldCat.org] (P p)

Original publications

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)