PycA
- Description: pyruvate carboxylase
Gene name | pycA |
Synonyms | ylaP |
Essential | no |
Product | pyruvate carboxylase |
Function | replenishment of the oxaloacetate pool |
MW, pI | 127 kDa, 5.407 |
Gene length, protein length | 3444 bp, 1148 aa |
Immediate neighbours | ftsW, ctaA |
Gene sequence (+200bp) | Protein sequence |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Coordinates:
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):
- Effectors of protein activity:
- Interactions:
- Localization: membrane associated PubMed
Database entries
- Structure: 3BG5 (S. aureus)
- Swiss prot entry:
- 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.
PycA is subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Sigma factor:
- 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
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed