RnpA

• Description: protein component of RNase 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

Categories containing this gene/protein

Rnases, translation, essential genes

The gene

Basic information

• Locus tag: BSU41050

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor (according to Swiss-Prot)

• Protein family: rnpA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: RnpA-RpmH, RnpA-RnpB

• Localization:

Database entries

• Structure: 1A6F, 1AF6 PubMed

• UniProt: P25814

• KEGG entry: [2]

• E.C. number: 3.1.26.5

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

• Carol Fierke, University of Michigan, Ann Arbor, USA homepage
• Roland Hartmann, Marburg University, Germany homepage

References

Reviews

Roland K Hartmann, Markus Gössringer, Bettina Späth, Susan Fischer, Anita Marchfelder
The making of tRNAs and more - RNase P and tRNase Z.
Prog Mol Biol Transl Sci: 2009, 85;319-68
[PubMed:19215776] [WorldCat.org] [DOI] (P p)

J Kristin Smith, John Hsieh, Carol A Fierke
Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.
Biopolymers: 2007, 87(5-6);329-38
[PubMed:17868095] [WorldCat.org] [DOI] (P p)

Alexei V Kazantsev, Norman R Pace
Bacterial RNase P: a new view of an ancient enzyme.
Nat Rev Microbiol: 2006, 4(10);729-40
[PubMed:16980936] [WorldCat.org] [DOI] (I p)

Donald Evans, Steven M Marquez, Norman R Pace
RNase P: interface of the RNA and protein worlds.
Trends Biochem Sci: 2006, 31(6);333-41
[PubMed:16679018] [WorldCat.org] [DOI] (P p)

Alfredo Torres-Larios, Kerren K Swinger, Tao Pan, Alfonso Mondragón
Structure of ribonuclease P--a universal ribozyme.
Curr Opin Struct Biol: 2006, 16(3);327-35
[PubMed:16650980] [WorldCat.org] [DOI] (P p)

John Hsieh, Andy J Andrews, Carol A Fierke
Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P.
Biopolymers: 2004, 73(1);79-89
[PubMed:14691942] [WorldCat.org] [DOI] (P p)

Enno Hartmann, Roland K Hartmann
The enigma of ribonuclease P evolution.
Trends Genet: 2003, 19(10);561-9
[PubMed:14550630] [WorldCat.org] [DOI] (P p)

L A Kirsebom, A Vioque
RNase P from bacteria. Substrate recognition and function of the protein subunit.
Mol Biol Rep: 1995, 22(2-3);99-109
[PubMed:8901495] [WorldCat.org] [DOI] (P p)