DP00387: Ribonuclease P protein componentFASTA viewXML view

General information
DisProt:DP00387
Name:Ribonuclease P protein component
Synonym(s):RNPA_BACSU
RNaseP protein
RNase P protein
EC 3.1.26.5
Protein C5
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P25814
UniGene: 
SwissProt: RNPA_BACSU
TrEMBL:  
NCBI (GI): 585905
Source organism:Bacillus subtilis
Sequence length:116
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK IGNAVMRNRI - 60
KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL QHLFRKSSLY KKSSSK



Functional narrative    

Ribonuclease P (RNase P) is the endoribonuclease responsible for the 5-prime-maturation of precursor tRNA transcripts. In bacteria, RNase P is composed of a catalytic RNA subunit and an associated protein subunit that enhances the substrate specificity of the holoenzyme. RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.

Region 1: 1-116

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 116
Length:116
Region sequence:

MKKRNRLKKNEDFQKVFKHGTSVANRQFVLYTLDQPENDELRVGLSVSKKIGNAVMRNRI
KRLIRQAFLEEKERLKEKDYIIIARKPASQLTYEETKKSLQHLFRKSSLYKKSSSK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises from the ordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-genomic RNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (310 K; )

  2. Circular dichroism (CD) spectroscopy, near-UV (310 K; )

  3. Nuclear magnetic resonance (NMR) (301 K; D20 (10%); Sodium cacodylate (pH 7.0) 10 mM; TMSP 20 ug/ml)
References:
  1. Henkels CH, Kurz JC, Fierke CA, Oas TG. "Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein." Biochemistry. 2001; 40(9): 2777-89. PubMed: 11258888

  2. Henkels CH, Oas TG. "Thermodynamic Characterization of the Osmolyte- and Ligand-Folded States of Bacillus subtilis Ribonuclease P Protein." Biochemistry. 2005; 44(39): 13014-26. PubMed: 16185070
Comments:
RNase P is predominantly unfolded when isolated from RNA and small molecule anions in a low-ionic strength buffer. The P protein can be induced to refold by increasing the anion concentration in solution or by the addition of the osmolyte trimethylamine N-oxide (TMAO).


Comments


Ribonuclease P (RNase P) is the endoribonuclease responsible for the 5-prime-maturation of precursor tRNA transcripts. In bacteria, RNase P is composed of a catalytic RNA subunit and an associated protein subunit that enhances the substrate specificity of the holoenzyme.


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