Difference between revisions of "RnpA"

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Line 82: Line 82:
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P25814 P25814]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P25814 P25814]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU41050]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU41050 BSU41050]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.1.26.5 3.1.26.5]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.1.26.5 3.1.26.5]

Revision as of 23:53, 13 May 2009

  • Description: protein component of ribonuclease P

Gene name rnpA
Synonyms
Essential yes PubMed
Product protein component of RNase P (substrate specificity)
Function cleavage of precursor sequences
from the 5' ends of pre-tRNAs
MW, pI 13 kDa, 10.804
Gene length, protein length 348 bp, 116 aa
Immediate neighbours spoIIIJ, rpmH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThdF jag spoIIIJ rnpA rpmH context.png
This image was kindly provided by SubtiList




The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

essential PubMed

Database entries

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

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:

Database entries

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Roland Hartmann, Marburg University, Germany homepage

Your additional remarks

References

  1. Hansen, A., Pfeiffer, T., Zuleeg, T., Limmer, S., Ciesiolka, J., Feltens, R. & Hartmann, R. K. (2001). Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzyme from Escherichia coli and Bacillus subtilis. Mol Microbiol 41, 131-143. PubMed
  2. Stams T, Niranjanakumari S, Fierke CA, Christianson DW (1998) Ribonuclease P protein structure: evolutionary origins in the translational apparatus.Science 280: 752-755. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed