Difference between revisions of "Sandbox"
| Line 1: | Line 1: | ||
| − | * '''Description:''' heat-shock protein ( | + | * '''Description:''' class I heat-shock protein (molecular chaperone) <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
| − | |'' | + | |''dnaK'' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | ||
| Line 10: | Line 10: | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || heat-shock protein ( | + | |style="background:#ABCDEF;" align="center"| '''Product''' || class I heat-shock protein (molecular chaperone) |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || protein quality control | |style="background:#ABCDEF;" align="center"|'''Function''' || protein quality control | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 65 kDa, 4.571 |
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1833 bp, 611 aa |
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[surC]]'', ''[[grpE]]'' |
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS: | + | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB14489]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
|- | |- | ||
| − | + | |colspan="2" | '''Genetic context''' <br/> [[Image:dnaK_context.gif]] | |
| − | |||
| − | |colspan="2" | '''Genetic context''' <br/> [[Image: | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
| Line 45: | Line 43: | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/lepA-hemN-hrcA-grpE-dnaKJ-yqeTUV.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/lepA-hemN-hrcA-grpE-dnaKJ-yqeTUV.html] | ||
| − | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+ | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10664] |
=== Additional information=== | === Additional information=== | ||
| Line 66: | Line 64: | ||
* '''Domains:''' | * '''Domains:''' | ||
| − | * '''Modification:''' | + | * '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
| Line 74: | Line 72: | ||
* '''Interactions:''' [[DnaK]]-[[DnaJ]] | * '''Interactions:''' [[DnaK]]-[[DnaJ]] | ||
| − | * '''Localization:''' Cytoplasm | + | * '''Localization:''' Cytoplasm Membrane-proximal (Spotty) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] |
=== Database entries === | === Database entries === | ||
| Line 82: | Line 80: | ||
* '''Swiss prot entry:''' | * '''Swiss prot entry:''' | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU25470] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
| Line 122: | Line 120: | ||
=References= | =References= | ||
| + | # Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in ''Bacillus subtilis''. ''Proteomics'' '''7:''' 3509-3526. [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
| + | # Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in ''Bacillus subtilis'': identification of new proteins at the DNA replication factory ''Proteomics'' '''6:''' 2135-2146. [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] | ||
# Wetzstein, M., U. Völker, J. Dedio, S. Löbau, U. Zuber, M. Schiesswohl, C. Herget, M. Hecker, and W. Schumann. 1992. Cloning, sequencing, and molecular analysis of the ''dnaK'' locus from ''Bacillus subtilis''. J. Bacteriol. 174:3300-3310. [http://www.ncbi.nlm.nih.gov/sites/entrez/1339421 PubMed] | # Wetzstein, M., U. Völker, J. Dedio, S. Löbau, U. Zuber, M. Schiesswohl, C. Herget, M. Hecker, and W. Schumann. 1992. Cloning, sequencing, and molecular analysis of the ''dnaK'' locus from ''Bacillus subtilis''. J. Bacteriol. 174:3300-3310. [http://www.ncbi.nlm.nih.gov/sites/entrez/1339421 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 02:57, 30 April 2009
- 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 |
| MW, pI | 65 kDa, 4.571 |
| Gene length, protein length | 1833 bp, 611 aa |
| Immediate neighbours | surC, grpE |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Coordinates:
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization: Cytoplasm Membrane-proximal (Spotty) PubMed
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation: induced by heat shock PubMed
- Regulatory mechanism: repressed at normal temperature by HrcA
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Wolfgang Schumann, Bayreuth University, Germany Homepage
Your additional remarks
References
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
- Wetzstein, M., U. Völker, J. Dedio, S. Löbau, U. Zuber, M. Schiesswohl, C. Herget, M. Hecker, and W. Schumann. 1992. Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis. J. Bacteriol. 174:3300-3310. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
