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

• 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

• 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

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Frieder Merz, Daniel Boehringer, Christiane Schaffitzel, Steffen Preissler, Anja Hoffmann, Timm Maier, Anna Rutkowska, Jasmin Lozza, Nenad Ban, Bernd Bukau, Elke Deuerling
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome.
EMBO J: 2008, 27(11);1622-32
[PubMed:18497744] [WorldCat.org] [DOI] (I p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Frank Schlünzen, Daniel N Wilson, Pingsheng Tian, Jörg M Harms, Stuart J McInnes, Harly A S Hansen, Renate Albrecht, Jörg Buerger, Sigurd M Wilbanks, Paola Fucini
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction.
Structure: 2005, 13(11);1685-94
[PubMed:16271892] [WorldCat.org] [DOI] (P p)

David Baram, Erez Pyetan, Assa Sittner, Tamar Auerbach-Nevo, Anat Bashan, Ada Yonath
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action.
Proc Natl Acad Sci U S A: 2005, 102(34);12017-22
[PubMed:16091460] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Günter Kramer, Thomas Rauch, Wolfgang Rist, Sonja Vorderwülbecke, Holger Patzelt, Agnes Schulze-Specking, Nenad Ban, Elke Deuerling, Bernd Bukau
L23 protein functions as a chaperone docking site on the ribosome.
Nature: 2002, 419(6903);171-4
[PubMed:12226666] [WorldCat.org] [DOI] (P p)

Dindo Y Reyes, Hirofumi Yoshikawa
DnaK chaperone machine and trigger factor are only partially required for normal growth of Bacillus subtilis.
Biosci Biotechnol Biochem: 2002, 66(7);1583-6
[PubMed:12224648] [WorldCat.org] [DOI] (P p)

S F Göthel, C Scholz, F X Schmid, M A Marahiel
Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.
Biochemistry: 1998, 37(38);13392-9
[PubMed:9748346] [WorldCat.org] [DOI] (P p)

S F Göthel, R Schmid, A Wipat, N M Carter, P T Emmerson, C R Harwood, M A Marahiel
An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor.
Eur J Biochem: 1997, 244(1);59-65
[PubMed:9063446] [WorldCat.org] [DOI] (P p)

A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504] [WorldCat.org] [DOI] (P p)