Difference between revisions of "CspD"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[RNA chaperones]]}},
 
{{SubtiWiki category|[[RNA chaperones]]}},
{{SubtiWiki category|[[cold stress proteins]]}}
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{{SubtiWiki category|[[cold stress proteins]]}},
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[[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===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''
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* '''[[Domains]]:'''
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[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=cspD_2307905_2308105_1 cspD] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cspD_2307905_2308105_1 cspD] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
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* '''Additional information:'''  
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** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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<pubmed>12171653,12838604,</pubmed>
 
<pubmed>12171653,12838604,</pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>12399512,11752341,11717297,9920884,12427936,11591689,9379903,17981983, </pubmed>
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<pubmed>12399512,11752341,11717297,9920884,12427936,11591689,9379903,17981983, 15378759</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:53, 5 March 2014

  • Description: cold shock protein

Gene name cspD
Synonyms
Essential no
Product cold shock protein
Function RNA chaperone
Gene expression levels in SubtiExpress: cspD
MW, pI 7 kDa, 4.31
Gene length, protein length 198 bp, 66 aa
Immediate neighbours ugtP, degR
Sequences Protein DNA DNA_with_flanks
Genetic context
CspD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CspD expression.png















Categories containing this gene/protein

RNA chaperones, cold stress proteins, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU21930

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
    • weakly induced by cold shock PubMed
  • Regulatory mechanism:

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

Your additional remarks

References

Reviews

Michael H Weber, Mohamed A Marahiel
Bacterial cold shock responses.
Sci Prog: 2003, 86(Pt 1-2);9-75
[PubMed:12838604] [WorldCat.org] [DOI] (P p)

Michael H W Weber, Mohamed A Marahiel
Coping with the cold: the cold shock response in the Gram-positive soil bacterium Bacillus subtilis.
Philos Trans R Soc Lond B Biol Sci: 2002, 357(1423);895-907
[PubMed:12171653] [WorldCat.org] [DOI] (P p)

Original publications

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I 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)

Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading): 2002, 148(Pt 11);3441-3455
[PubMed:12427936] [WorldCat.org] [DOI] (P p)

Carsten L Beckering, Leif Steil, Michael H W Weber, Uwe Völker, Mohamed A Marahiel
Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.
J Bacteriol: 2002, 184(22);6395-402
[PubMed:12399512] [WorldCat.org] [DOI] (P p)

Michael H W Weber, Ingo Fricke, Niclas Doll, Mohamed A Marahiel
CSDBase: an interactive database for cold shock domain-containing proteins and the bacterial cold shock response.
Nucleic Acids Res: 2002, 30(1);375-8
[PubMed:11752341] [WorldCat.org] [DOI] (I p)

M H Weber, C L Beckering, M A Marahiel
Complementation of cold shock proteins by translation initiation factor IF1 in vivo.
J Bacteriol: 2001, 183(24);7381-6
[PubMed:11717297] [WorldCat.org] [DOI] (P p)

M H Weber, A V Volkov, I Fricke, M A Marahiel, P L Graumann
Localization of cold shock proteins to cytosolic spaces surrounding nucleoids in Bacillus subtilis depends on active transcription.
J Bacteriol: 2001, 183(21);6435-43
[PubMed:11591689] [WorldCat.org] [DOI] (P p)

T Schindler, P L Graumann, D Perl, S Ma, F X Schmid, M A Marahiel
The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo.
J Biol Chem: 1999, 274(6);3407-13
[PubMed:9920884] [WorldCat.org] [DOI] (P p)

P Graumann, T M Wendrich, M H Weber, K Schröder, M A Marahiel
A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures.
Mol Microbiol: 1997, 25(4);741-56
[PubMed:9379903] [WorldCat.org] [DOI] (P p)