Difference between revisions of "Tig"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[chaperones/ protein folding]]}}, | ||
| + | {{SubtiWiki category|[[phosphoproteins]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[stringent response]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 22:06, 8 December 2010
- 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
| |
Contents
Categories containing this gene/protein
chaperones/ protein folding, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28230
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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
- 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
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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)
Original publications
