Difference between revisions of "DnaK"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || protein quality control | |style="background:#ABCDEF;" align="center"|'''Function''' || protein quality control | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU25470 dnaK] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/DnaK DnaK] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/DnaK DnaK] | ||
| Line 26: | Line 26: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[surC]]'', ''[[grpE]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[surC]]'', ''[[grpE]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU25470 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU25470 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU25470 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:dnaK_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:dnaK_context.gif]] | ||
Revision as of 13:20, 13 May 2013
- 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: Stress | |
| MW, pI | 65 kDa, 4.571 |
| Gene length, protein length | 1833 bp, 611 aa |
| Immediate neighbours | surC, grpE |
| Sequences | Protein DNA Advanced_DNA |
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
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:
- Domains:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P17820
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
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
Additional publications: PubMed
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)
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)
