PabA

• 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
Gene expression levels in SubtiExpress: pabA
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions: PabA-PabB, PabA-TrpE

• Localization:

Database entries

• Structure:

• UniProt: P28819

• KEGG entry: [3]

• E.C. number: 2.6.1.85

Expression and regulation

• Operon: pabB-pabA-pabC-sul-folB-folK-yazB-yacF-lysS PubMed

• Expression browser: pabA PubMed

• Sigma factor: SigA PubMed

• Regulation: translation repressed by tryptophan (MtrB) PubMed

• Regulatory mechanism: MtrB: translation termination PubMed

• Additional information:
  • the pabA-pabC part of the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Helen Yakhnin, Alexander V Yakhnin, Paul Babitzke
Translation control of trpG from transcripts originating from the folate operon promoter of Bacillus subtilis is influenced by translation-mediated displacement of bound TRAP, while translation control of transcripts originating from a newly identified trpG promoter is not.
J Bacteriol: 2007, 189(3);872-9
[PubMed:17114263] [WorldCat.org] [DOI] (P p)

Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182] [WorldCat.org] [DOI] (P p)

C Baumann, J Otridge, P Gollnick
Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.
J Biol Chem: 1996, 271(21);12269-74
[PubMed:8647825] [WorldCat.org] [DOI] (P p)

P Babitzke, J T Stults, S J Shire, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts.
J Biol Chem: 1994, 269(24);16597-604
[PubMed:7515880] [WorldCat.org] (P p)