Difference between revisions of "ProS"

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(Extended information on the protein)
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* '''Locus tag:''' BSU16570
 
* '''Locus tag:''' BSU16570
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[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=proS_1725330_1727024_1 Expression]
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 09:47, 25 January 2012

  • Description: prolyl-tRNA synthetase

Gene name proS
Synonyms
Essential yes PubMed
Product prolyl-tRNA synthetase
Function translation
Metabolic function and regulation of this protein in SubtiPathways:
tRNA charging
MW, pI 63 kDa, 5.012
Gene length, protein length 1692 bp, 564 aa
Immediate neighbours rasP, polC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ProS context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16570

Expression

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:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

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)