rnpA RNase P protein component [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: rnpA
Official Full Name: RNase P protein component
Primary source: ECOCYC:EG10862
Locus tag: b3704
See related: ASAP:ABE-0012117
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK3696
Summary: Has leadzyme properties. [More information is available at EcoGene: EG10862]. RnpB RNA and RnpA protein together compose ribonuclease P (RNAse P) . [More information is available at EcoCyc: EG10862].
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Genomic context

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Sequence:: NC_000913.3 (3884493..3884852)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Inactivation of RNase P in Escherichia coli significantly changes post-transcriptional RNA metabolism.
Title: Inactivation of RNase P in Escherichia coli significantly changes post-transcriptional RNA metabolism.
The results demonstrate that directional processing is an intrinsic property of RNase P and show how RNA sequence and structure context can modulate reaction rates in order to direct precursors along specific pathways.
Title: Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.
findings demonstrate the rph-1 mutation leads to synthesis of a truncated functionally inactive RNase PH protein that interferes with the 5'-end maturation of specific tRNAs with short 5' leaders by RNase P in the absence of RppH an RNA pyrophosphohydrolase that converts primary 5' triphosphates into 5' monophosphates; data indicate the presence of the triphosphate interferes with RNase P binding to the pre-tRNA
Title: The rph-1-Encoded Truncated RNase PH Protein Inhibits RNase P Maturation of Pre-tRNAs with Short Leader Sequences in the Absence of RppH.
The comparative biology of Escherichia coli RNase P and Arabidopsis thaliana PRORP isozymes has been reported.
Title: Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.
The ability of RNase P to initiate tRNA processing at the 3' ends of long primary transcripts by endonucleolytically removing the Rho-independent transcription terminator represents a previously unidentified function for the enzyme.
Title: Processing of the seven valine tRNAs in Escherichia coli involves novel features of RNase P.
Rules govern substrate recognition by C5, which reveal specificity that is hidden in cellular substrates for RNase P; nonspecific and specific RNA-binding modes may not differ fundamentally, but represent distinct parts of common affinity distributions.
Title: Hidden specificity in an apparently nonspecific RNA-binding protein.
C5 protein has evolved to compensate for tRNA variation at positions important for binding to P RNA, allowing for tRNA specialization
Title: Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair.
These results demonstrate that the C5 protein metabolically stabilizes M1 RNA in the cell.
Title: Novel function of C5 protein as a metabolic stabilizer of M1 RNA.
Description for the first time of a previously unidentified pathway for the maturation of tRNAs in polycistronic operons where the processing of the primary transcripts only involves RNase P.
Title: Ribonuclease P processes polycistronic tRNA transcripts in Escherichia coli independent of ribonuclease E.
Cognate protein subunit C5 enhances metal ion affinity in the active site of RNAase P, and thus is likely to contribute significantly to rate enhancement at physiological metal ion concentrations.
Title: Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 3'-tRNA processing endoribonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables endonuclease activity	IEA Inferred from Electronic Annotation more info
enables ribonuclease P activity	IBA Inferred from Biological aspect of Ancestor more info
enables ribonuclease P activity	IEA Inferred from Electronic Annotation more info
enables tRNA binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within RNA processing	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within RNA processing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA 3'-end processing	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within tRNA 5'-leader removal	IDA Inferred from Direct Assay more info	PubMed
involved_in tRNA 5'-leader removal	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within tRNA processing	EXP Inferred from Experiment more info	PubMed
involved_in tRNA processing	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of ribonuclease P complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonuclease P complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: RNase P protein component

NP_418159.1

EC 3.1.26.5

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

3884493..3884852

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_418159.1 RNase P protein component [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_418159.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A5B9AV07

Conserved Domains (1) summary

PRK01732
Location:1 → 114

rnpA; ribonuclease P; Reviewed