CspD
-  Description: cold shock protein 
| Gene name | cspD | 
| Synonyms | |
| Essential | no | 
| Product | cold shock protein | 
| Function | RNA chaperone | 
| MW, pI | 7 kDa, 4.31 | 
| Gene length, protein length | 198 bp, 66 aa | 
| Immediate neighbours | ugtP, degR | 
| Get the DNA and protein sequences (Barbe et al., 2009) | |
| Genetic context    This image was kindly provided by SubtiList | |
Contents
Categories containing this gene/protein
RNA chaperones, cold stress 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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P51777
- 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:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation 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
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)
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)

