Difference between revisions of "Sandbox"
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− | * '''Description:''' | + | * '''Description:''' major cold-shock protein <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''' | ||
− | |'' | + | |''cspB'' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || major cold-shock protein |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || RNA chaperone |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 7 kDa, 4.341 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 201 bp, 67 aa |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yhcI]]'', ''[[yhcJ]]'' |
|- | |- | ||
− | |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:CAB12738]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
|- | |- | ||
− | |colspan="2" | '''Genetic context''' <br/> [[Image: | + | |colspan="2" | '''Genetic context''' <br/> [[Image:cspB_context.gif]] |
<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> | ||
|- | |- | ||
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU09100 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
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=== Database entries === | === Database entries === | ||
− | * '''DBTBS entry:''' | + | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cspB.html] |
− | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+ | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10824] |
=== Additional information=== | === Additional information=== | ||
Line 52: | Line 52: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' |
− | * '''Protein family:''' | + | * '''Protein family:''' |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''Interactions:''' [[CshB]]-[[CspB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed] |
− | * '''Localization:''' | + | * '''Localization:''' cytoplasm (according to Swiss-Prot), cytoplasma, colocalizes with the ribosomes [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed] |
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1CSQ 1CSQ], [http://www.rcsb.org/pdb/explore.do?structureId=1NMG 1NMG] (NMR) |
− | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/ | + | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P32081 P32081] |
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU09100] |
− | * '''E.C. number:''' | + | * '''E.C. number:''' |
=== Additional information=== | === Additional information=== | ||
+ | :* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
=Expression and regulation= | =Expression and regulation= | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] |
=Biological materials = | =Biological materials = | ||
Line 113: | Line 114: | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
+ | |||
+ | [[Mohamed Marahiel]], Marburg University, Germany [http://www.uni-marburg.de/fb15/fachgebiete/bio/marahiel?language_sync=1 homepage] | ||
=Your additional remarks= | =Your additional remarks= | ||
Line 118: | Line 121: | ||
=References= | =References= | ||
− | <pubmed> | + | <pubmed>16352840, </pubmed> |
− | # | + | # Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] |
+ | # Hunger, K., Beckering, C. L., Wiegeshoff, F., Graumann, P. L. & Marahiel, M. A. (2006). Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in ''Bacillus subtilis''. J Bacteriol. 188:240-248. [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 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 14:00, 8 June 2009
- Description: major cold-shock protein
Gene name | cspB |
Synonyms | |
Essential | no |
Product | major cold-shock protein |
Function | RNA chaperone |
MW, pI | 7 kDa, 4.341 |
Gene length, protein length | 201 bp, 67 aa |
Immediate neighbours | yhcI, yhcJ |
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: BSU09100
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:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot), cytoplasma, colocalizes with the ribosomes PubMed
Database entries
- Swiss prot entry: P32081
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon:
- Regulation:
- 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
Mohamed Marahiel, Marburg University, Germany homepage
Your additional remarks
References
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Hunger, K., Beckering, C. L., Wiegeshoff, F., Graumann, P. L. & Marahiel, M. A. (2006). Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis. J Bacteriol. 188:240-248. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed