ProS

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  • Description: prolyl-tRNA synthetase

Gene name proS
Synonyms
Essential yes PubMed
Product prolyl-tRNA synthetase
Function translation
Gene expression levels in SubtiExpress: proS
Metabolic function and regulation of this protein in SubtiPathways:
proS
MW, pI 63 kDa, 5.012
Gene length, protein length 1692 bp, 564 aa
Immediate neighbours rasP, polC
Sequences Protein DNA DNA_with_flanks
Genetic context
ProS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ProS expression.png




























Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16570

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) (according to Swiss-Prot)
  • Protein family: ProS type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2I4L (from Rhodopseudomonas palustris, 51% identity, 71% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 784 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2694 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Thibaut Crepin, Anna Yaremchuk, Mikhail Tukalo, Stephen Cusack
Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain.
Structure: 2006, 14(10);1511-25
[PubMed:17027500] [WorldCat.org] [DOI] (P p)