Difference between revisions of "PycA"

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

Revision as of 13:40, 8 December 2014

  • 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:
pycA
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:
  • 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
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2222 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 6831 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1602 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 907 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2037 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] [DOI] (P p)

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

Original publications