Difference between revisions of "DnaK"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[chaperones/ protein folding]]}}, | {{SubtiWiki category|[[chaperones/ protein folding]]}}, | ||
{{SubtiWiki category|[[heat shock proteins]]}}, | {{SubtiWiki category|[[heat shock proteins]]}}, | ||
| − | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | * '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaK_2626112_2627947_-1 dnaK] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaK_2626112_2627947_-1 dnaK] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|1339421}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|1339421}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | + | <pubmed>1339421,12224648,10383760,9023197,7540247,7592421 ,16479537, 1339421 ,17726680 22268681 15378759</pubmed> | |
| − | <pubmed>1339421,12224648,10383760,9023197,7540247,7592421 ,16479537, 1339421 ,17726680 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:36, 5 March 2014
- Description: class I heat-shock protein (molecular chaperone)
| Gene name | dnaK |
| Synonyms | |
| Essential | no |
| Product | class I heat-shock protein (molecular chaperone) |
| Function | protein quality control |
| Gene expression levels in SubtiExpress: dnaK | |
| Interactions involving this protein in SubtInteract: DnaK | |
| Metabolic function and regulation of this protein in SubtiPathways: dnaK | |
| MW, pI | 65 kDa, 4.571 |
| Gene length, protein length | 1833 bp, 611 aa |
| Immediate neighbours | surC, grpE |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
chaperones/ protein folding, heat shock proteins, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU25470
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: heat shock protein 70 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P17820
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Wolfgang Schumann, Bayreuth University, Germany Homepage
Your additional remarks
References
G Seydlová, P Halada, R Fišer, O Toman, A Ulrych, J Svobodová
DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress.
J Appl Microbiol: 2012, 112(4);765-74
[PubMed:22268681]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[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)
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)
G Homuth, A Mogk, W Schumann
Post-transcriptional regulation of the Bacillus subtilis dnaK operon.
Mol Microbiol: 1999, 32(6);1183-97
[PubMed:10383760]
[WorldCat.org]
[DOI]
(P p)
G Homuth, S Masuda, A Mogk, Y Kobayashi, W Schumann
The dnaK operon of Bacillus subtilis is heptacistronic.
J Bacteriol: 1997, 179(4);1153-64
[PubMed:9023197]
[WorldCat.org]
[DOI]
(P p)
G Yuan, S L Wong
Isolation and characterization of Bacillus subtilis groE regulatory mutants: evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaK.
J Bacteriol: 1995, 177(22);6462-8
[PubMed:7592421]
[WorldCat.org]
[DOI]
(P p)
A Schulz, B Tzschaschel, W Schumann
Isolation and analysis of mutants of the dnaK operon of Bacillus subtilis.
Mol Microbiol: 1995, 15(3);421-9
[PubMed:7540247]
[WorldCat.org]
[DOI]
(P p)
M Wetzstein, U Völker, J Dedio, S Löbau, U Zuber, M Schiesswohl, C Herget, M Hecker, W Schumann
Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis.
J Bacteriol: 1992, 174(10);3300-10
[PubMed:1339421]
[WorldCat.org]
[DOI]
(P p)
