Difference between revisions of "RnpA"
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 This image was kindly provided by SubtiList
|
Contents
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
- Swiss prot entry: P25814
- KEGG entry: BSU41050
- E.C. number: 3.1.26.5
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
- 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
- Stams T, Niranjanakumari S, Fierke CA, Christianson DW (1998) Ribonuclease P protein structure: evolutionary origins in the translational apparatus.Science 280: 752-755. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed