Difference between revisions of "Tig"
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=Expression and regulation= | =Expression and regulation= | ||
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* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
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=References= | =References= | ||
| − | <pubmed>12224648,9748346,9063446,,16493705, </pubmed> | + | <pubmed>12224648,9748346,9063446,,16493705, 8969504 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 21:17, 13 December 2009
- 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
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
- Structure:
- 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: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)
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)
