CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003042
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease P protein component 
Protein Synonyms/Alias
 RNase P protein; RNaseP protein; Protein C5 
Gene Name
 rnpA 
Gene Synonyms/Alias
 b3704; JW3681 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
107ALSEALEKLWRRHCRacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 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. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 119 AA 
Protein Sequence
MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH 60
ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS 119 
Gene Ontology
 GO:0004526; F:ribonuclease P activity; IDA:EcoCyc.
 GO:0000049; F:tRNA binding; IEA:InterPro.
 GO:0001682; P:tRNA 5'-leader removal; IDA:EcoliWiki. 
Interpro
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR000100; RNase_P.
 IPR020539; RNase_P_CS. 
Pfam
 PF00825; Ribonuclease_P 
SMART
  
PROSITE
 PS00648; RIBONUCLEASE_P 
PRINTS