Difference between revisions of "TrpA"

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Revision as of 12:05, 19 April 2012

  • Description: tryptophan synthase (alpha subunit)

Gene name trpA
Synonyms
Essential no
Product tryptophan synthase (alpha subunit)
Function biosynthesis of tryptophan
Interactions involving this protein in SubtInteract: TrpA
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
MW, pI 29 kDa, 4.817
Gene length, protein length 801 bp, 267 aa
Immediate neighbours hisC, trpB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TrpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TrpA expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

  • Locus tag: BSU22630

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O (according to Swiss-Prot)
  • Protein family: UPF0403 family (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: 1WQ5 (from Escherichia coli, 35% identity, 53% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947