pnp polynucleotide phosphorylase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: pnp
Official Full Name: polynucleotide phosphorylase
Primary source: ECOCYC:EG10743
Locus tag: b3164
See related: ASAP:ABE-0010397
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: bfl; ECK3152
Summary: Cold induction occurs by reversal of post-translational autoregulation. [More information is available at EcoGene: EG10743]. Polynucleotide phosphorylase (PNPase) is a 3' to 5' exonuclease and a 3'-terminal oligonucleotide polymerase. [More information is available at EcoCyc: EG10743].
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Genomic context

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Sequence:: NC_000913.3 (3309033..3311168, complement)

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

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments.
Title: Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments.
Inhibition of homologous PNPase by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.
Title: Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.
PNPase and RNase PH facilitate the stability and regulatory function of the sRNAs RyhB, CyaR, and MicA during exponential growth.
Title: The Phosphorolytic Exoribonucleases Polynucleotide Phosphorylase and RNase PH Stabilize sRNAs and Facilitate Regulation of Their mRNA Targets.
PNPase regulates its own expression via a reversible RNase III-independent pathway acting upstream from the RNase III-dependent branch.
Title: RNase III-Independent Autogenous Regulation of Escherichia coli Polynucleotide Phosphorylase via Translational Repression.
A conserved loop in polynucleotide phosphorylase (PNPase) is essential for both RNA and ADP/phosphate binding.
Title: A conserved loop in polynucleotide phosphorylase (PNPase) essential for both RNA and ADP/phosphate binding.
These results demonstrate that polynucleotide phosphorylase is necessary to maintain bacterial cells in the planktonic mode through down-regulation of pgaABCD expression and PNAG production.
Title: The RNA processing enzyme polynucleotide phosphorylase negatively controls biofilm formation by repressing poly-N-acetylglucosamine (PNAG) production in Escherichia coli C.
S1 and KH domains of pnp determine the efficiency of RNA binding and autoregulation.
Title: S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and autoregulation.
Spontaneous mutations resulting from replication errors, which are normally repaired by the mismatch repair (MMR) system, are sharply reduced in a polynucleotide phosphorylase-deficient Escherichia coli strain.
Title: Polynucleotide phosphorylase plays an important role in the generation of spontaneous mutations in Escherichia coli.
Absence of PNPase decreases the survival of cells exposed to UV radiation.
Title: Involvement of pnp in survival of UV radiation in Escherichia coli K-12.
Role of polynucleotide phosphorylase in sRNA function in Escherichia coli
Title: Role of polynucleotide phosphorylase in sRNA function in Escherichia coli.

Submit: New GeneRIF Correction See all GeneRIFs (20)

Pathways from PubChem

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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'-5'-RNA exonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables 3'-5'-RNA exonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables RNA binding	EXP Inferred from Experiment more info	PubMed
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	IPI Inferred from Physical Interaction more info	PubMed
enables cyclic-di-GMP binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nucleotidyltransferase activity	IEA Inferred from Electronic Annotation more info
enables polyribonucleotide nucleotidyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables polyribonucleotide nucleotidyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables polyribonucleotide nucleotidyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in RNA catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in RNA catabolic process	NAS Non-traceable Author Statement more info	PubMed
involved_in RNA processing	IEA Inferred from Electronic Annotation more info
involved_in RNA processing	NAS Non-traceable Author Statement more info	PubMed
involved_in mRNA catabolic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to heat	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of bacterial degradosome	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	HDA more info	PubMed
located_in membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: polynucleotide phosphorylase

NP_417633.4

EC 2.7.7.8

EC 3.1.13.1

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

3309033..3311168 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417633.4 polynucleotide phosphorylase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417633.4

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A8S7QZ98

Conserved Domains (1) summary

PRK11824
Location:1 → 692

PRK11824; polynucleotide phosphorylase/polyadenylase; Provisional