MtrB

• Description: tryptophan operon RNA-binding attenuation protein (TRAP)
  
  

Gene name	mtrB
Synonyms
Essential	no
Product	tryptophan operon RNA-binding attenuation protein (TRAP)
Function	regulation of tryptophan biosynthesis (and translation) attenuation in the trp operon); repression of the folate operon
MW, pI	8 kDa, 7.333
Gene length, protein length	225 bp, 75 aa
Immediate neighbours	hepS, mtrA
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: BSU22770

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: prpD family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: MtrB-RtpA

• Localization:

Database entries

• Structure: 2ZD0 (mutant TRAP, Geobacillus stearothermophilus), 1WAP (complex with L-tryptophan)

• Swiss prot entry: P19466

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

P Babitzke, P Gollnick
Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure.
J Bacteriol: 2001, 183(20);5795-802
[PubMed:11566976] [WorldCat.org] [DOI] (P p)

A A Antson, E J Dodson, G Dodson, R B Greaves, X Chen, P Gollnick
Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA.
Nature: 1999, 401(6750);235-42
[PubMed:10499579] [WorldCat.org] [DOI] (P p)

A A Antson, J Otridge, A M Brzozowski, E J Dodson, G G Dodson, K S Wilson, T M Smith, M Yang, T Kurecki, P Gollnick
The structure of trp RNA-binding attenuation protein.
Nature: 1995, 374(6524);693-700
[PubMed:7715723] [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)

1. Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P (1995) The structure of trp RNA-binding protein. Nature 374:693-700. PubMed
2. Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, Gollnick P (1999) Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401:235-242. PubMed
3. Babitzke P, Gollnick P (2001) Posttransription iniation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure. J Bacteriol 183:5795-5802. PubMed
4. Babitzke P, Stults JT, Shire SJ, Yanofsky C (1994) 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 269:16597-16604. PubMed
5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed