TrpE

• Description: anthranilate synthase (subunit I)
  
  

Gene name	trpE
Synonyms
Essential	no
Product	anthranilate synthase (subunit I)
Function	biosynthesis of tryptophan
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp
MW, pI	57 kDa, 5.246
Gene length, protein length	1545 bp, 515 aa
Immediate neighbours	trpD, aroH
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU22680

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: subject to feedback inhibtion by tryptophan PubMed

• Interactions: PabA-TrpE

• Localization:

Database entries

• Structure:

• UniProt: P03963

• KEGG entry: [3]

• E.C. number: 4.1.3.27

Expression and regulation

• Operon: trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induction by tryptophan ( TRAP) PubMed

• Regulatory mechanism:
  • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed

• Additional information:
  • subject to feedback inhibtion by tryptophan PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Adam P McGraw, Ali Mokdad, François Major, Philip C Bevilacqua, Paul Babitzke
Molecular basis of TRAP-5'SL RNA interaction in the Bacillus subtilis trp operon transcription attenuation mechanism.
RNA: 2009, 15(1);55-66
[PubMed:19033375] [WorldCat.org] [DOI] (I p)

Adam P McGraw, Philip C Bevilacqua, Paul Babitzke
TRAP-5' stem loop interaction increases the efficiency of transcription termination in the Bacillus subtilis trpEDCFBA operon leader region.
RNA: 2007, 13(11);2020-33
[PubMed:17881743] [WorldCat.org] [DOI] (P 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)

Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255] [WorldCat.org] [DOI] (P p)

Paul Babitzke, Janell Schaak, Alexander V Yakhnin, Philip C Bevilacqua
Role of RNA structure in transcription attenuation in Bacillus subtilis: the trpEDCFBA operon as a model system.
Methods Enzymol: 2003, 371;392-404
[PubMed:14712717] [WorldCat.org] [DOI] (P p)

Janell E Schaak, Helen Yakhnin, Philip C Bevilacqua, Paul Babitzke
A Mg2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding.
J Mol Biol: 2003, 332(3);555-74
[PubMed:12963367] [WorldCat.org] [DOI] (P p)

H Yakhnin, J E Babiarz, A V Yakhnin, P Babitzke
Expression of the Bacillus subtilis trpEDCFBA operon is influenced by translational coupling and Rho termination factor.
J Bacteriol: 2001, 183(20);5918-26
[PubMed:11566991] [WorldCat.org] [DOI] (P p)

H Du, A V Yakhnin, S Dharmaraj, P Babitzke
trp RNA-binding attenuation protein-5' stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon.
J Bacteriol: 2000, 182(7);1819-27
[PubMed:10714985] [WorldCat.org] [DOI] (P p)

E Merino, P Babitzke, C Yanofsky
trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon.
J Bacteriol: 1995, 177(22);6362-70
[PubMed:7592410] [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)

J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914] [WorldCat.org] [DOI] (P p)

P Babitzke, C Yanofsky
Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein.
Proc Natl Acad Sci U S A: 1993, 90(1);133-7
[PubMed:7678334] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

M I Kuroda, D Henner, C Yanofsky
cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon.
J Bacteriol: 1988, 170(7);3080-8
[PubMed:3133360] [WorldCat.org] [DOI] (P p)

H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155] [WorldCat.org] [DOI] (P p)

D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737] [WorldCat.org] [DOI] (P p)

H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812] [WorldCat.org] [DOI] (P p)

E W Nester, R A Jensen
Control of aromatic acid biosynthesis in Bacillus subtilis: sequenial feedback inhibition.
J Bacteriol: 1966, 91(4);1594-8
[PubMed:4956345] [WorldCat.org] [DOI] (P p)