Difference between revisions of "PabA"

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(Extended information on the protein)
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* '''Additional information:'''
 
* '''Additional information:'''
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** the ''[[pabA]]-[[pabC]]'' part of the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
  
 
=Biological materials =
 
=Biological materials =
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<pubmed>16285852, 19385727</pubmed>
 
<pubmed>16285852, 19385727</pubmed>
 
==Original Publications==
 
==Original Publications==
 +
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 +
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
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<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
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[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
<pubmed>8647825,7515880,9084182,17114263  ,, </pubmed>
 
<pubmed>8647825,7515880,9084182,17114263  ,, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:39, 19 November 2011

  • Description: para-aminobenzoate synthase (subunit B)/ anthranilate synthase (subunit II)

Gene name pabA
Synonyms trpG, trpX
Essential no
Product para-aminobenzoate synthase (subunit B)/
anthranilate synthase (subunit II)
glutamine amidotransferase (subunit B)
and anthranilate synthase (subunit II)
Function biosynthesis of folate and tryptophan
Interactions involving this protein in SubtInteract: PabA
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp, Folate
MW, pI 21 kDa, 4.782
Gene length, protein length 582 bp, 194 aa
Immediate neighbours pabB, pabC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PabA context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, biosynthesis of cofactors

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

  • Locus tag: BSU00750

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: translation repressed by tryptophan (MtrB) PubMed
  • Regulatory mechanism: MtrB: translation termination PubMed
  • 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

Reviews

Paul Babitzke, Carol S Baker, Tony Romeo
Regulation of translation initiation by RNA binding proteins.
Annu Rev Microbiol: 2009, 63;27-44
[PubMed:19385727] [WorldCat.org] [DOI] (I p)

Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852] [WorldCat.org] [DOI] (P p)

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