Tig

• Description: trigger factor (prolyl isomerase)
  
  

Gene name	tig
Synonyms	yzzH
Essential	no
Product	trigger factor (prolyl isomerase)
Function	protein folding
MW, pI	47 kDa, 4.224
Gene length, protein length	1272 bp, 424 aa
Immediate neighbours	clpX, ysoA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

chaperones/ protein folding, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU28230

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Tig subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2VRH (the E. coli trigger factor) PubMed

• UniProt: P80698

• KEGG entry: [3]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: tig PubMed

• Expression browser: tig PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:
  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Carmela Giglione, Sonia Fieulaine, Thierry Meinnel
Cotranslational processing mechanisms: towards a dynamic 3D model.
Trends Biochem Sci: 2009, 34(8);417-26
[PubMed:19647435] [WorldCat.org] [DOI] (I p)

R D Wegrzyn, E Deuerling
Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding.
Cell Mol Life Sci: 2005, 62(23);2727-38
[PubMed:16231086] [WorldCat.org] [DOI] (P p)

Timm Maier, Lars Ferbitz, Elke Deuerling, Nenad Ban
A cradle for new proteins: trigger factor at the ribosome.
Curr Opin Struct Biol: 2005, 15(2);204-12
[PubMed:15837180] [WorldCat.org] [DOI] (P p)

Elke Deuerling, Bernd Bukau
Chaperone-assisted folding of newly synthesized proteins in the cytosol.
Crit Rev Biochem Mol Biol: 2004, 39(5-6);261-77
[PubMed:15763705] [WorldCat.org] [DOI] (P p)