Tig

• Description: trigger factor (prolyl isomerase)
  
  

Gene name	tig
Synonyms	yzzH
Essential	no
Product	trigger factor (prolyl isomerase)
Function	protein folding
Gene expression levels in SubtiExpress: tig
Interactions involving this protein in SubtInteract: Tig
MW, pI	47 kDa, 4.224
Gene length, protein length	1272 bp, 424 aa
Immediate neighbours	clpX, ysoA
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

chaperones/ protein folding, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU28230

Database entries

• BsubCyc: BSU28230

• 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 Arg-90 PubMed
  • phosphorylated on ser/ thr/ tyr PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • Tig-RplW PubMed
  • Tig-RpmC PubMed

• Localization:

Database entries

• BsubCyc: BSU28230

• 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
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 9318 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 56291 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 6608 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5389 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5836 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)