npr phosphorelay protein NPr [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: npr
Official Full Name: phosphorelay protein NPr
Primary source: ECOCYC:EG12147
Locus tag: b3206
See related: ASAP:ABE-0010524
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: ECK3195; ptsO; rpoR; yhbK
Summary: The rpoN operon contains rpoN-hpf-ptsN-yhbJ-npr. [More information is available at EcoGene: EG12147]. NPr, the product of ptsO, is homologous to the HPr protein of the phosphoenolpyruvate (PEP)-dependent carbohydrate phosphotransferase system (PTS) . [More information is available at EcoCyc: EG12147].
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Genomic context

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Sequence:: NC_000913.3 (3347966..3348238)

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?

The results presented here suggest a model in which SixA removes phosphoryl groups from the nitrogen-related phosphotransferase system by acting on NPr.
Title: The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System.
Study elucidated the structure of the NPr:EIN Ntr complex using a hybrid approach. The structure has a similar fold to the homologous HPr:EIN sugar complex, but differs in surface potential, which explains the difference in specificity between the two evolutionarily related enzyme pairs.
Title: Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.
Results suggest that the phosphoenolpyruvate hexose phosphotransferases PTS network serves as a global sensor of the sugar influx and also monitors the levels of several non-PTS compounds.
Title: Sugar Influx Sensing by the Phosphotransferase System of Escherichia coli.
these data suggest that unphosphorylated NPr decreases lipid A biosynthesis by inhibiting LpxD activity.
Title: Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD.
The deduced structure of NPr contains 3 alpha-helices and 4 beta-strands with the 3 helices all packed on the same face of the beta-sheet; the active site residue His16 of NPr for phosphoryl transfer was neutral and in the N epsilon 2-H tautomeric state.
Title: Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr.
The solution form of IIA(Ntr) from Escherichia coli and its interaction with its partner protein, NPr, were characterized by nuclear magnetic resonance spectroscopy.
Title: NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.

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General gene information

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Homology

Orthologs from OrthoDB

General protein information

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Preferred Names: phosphorelay protein NPr

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

3347966..3348238

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417673.1 phosphorelay protein NPr [Escherichia coli str. K-12 substr. MG1655]

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A376FXV2, A0A376VDU1

Conserved Domains (1) summary

PRK10897
Location:1 → 90

PRK10897; PTS phosphocarrier protein NPr