dosP oxygen-sensing c-di-GMP phosphodiesterase DosP [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Gene symbol: dosP
Gene description: oxygen-sensing c-di-GMP phosphodiesterase DosP
Primary source: ASAP:ABE-0004963
Locus tag: b1489
See related: ECOCYC:G6783
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: dos; ECK1483; pdeO; yddU
Summary: YddV/Dos may constitute a cyclic-di-GMP synthesis/degradation module (Mendez-Ortiz, 2006). [More information is available at EcoGene: EG13792]. Dos acts a direct sensor of oxygen; the protein has an N-terminal heme-binding PAS domain and a C-terminal phosphodiesterase domain . [More information is available at EcoCyc: G6783].
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Genomic context

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Sequence:: NC_000913.3 (1563334..1565733, 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

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

DosC is a diguanylate cyclase that synthesizes c-di-GMP from GTP, whereas DosP is a phosphodiesterase that linearizes c-di-GMP to pGpG. [review]
Title: Escherichia coli DosC and DosP: a role of c-di-GMP in compartmentalized sensing by degradosomes.
c-di-GMP positively modulates PgaD protein stability in a PgaC-dependent manner.
Title: Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated protein-protein interaction.
A phosphodiesterase (PDE) from Escherichia coli (Ec DOS) is a novel haem-based oxygen sensor enzyme.
Title: Catalysis and oxygen binding of Ec DOS: a haem-based oxygen-sensor enzyme from Escherichia coli.
These results suggest that YddV and Dos, through their opposite activities, fine-tune curli production in response to oxygen availability.
Title: The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli.
Phe113, residing near the O(2) molecule, has a critical role in optimizing the Fe(II)-O(2) complex for effective regulation of catalysis by DOS.
Title: Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment.
Examination of the catalytic activity of ferric complex-bound full-length Ec DOS in absence and presence of external ligands cyanide and imidazole shows that the heme at the sensor domain inhibits catalysis.
Title: Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding.
Data suggest that Arg97 plays critical roles in recognition of the O2 molecule and redox switching by stabilizing the Fe(II)-O2 complex.
Title: Arg97 at the heme-distal side of the isolated heme-bound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2.
the heme axial ligand, Met95, has a critical role in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP
Title: Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP.
expression of DOS(Ec) is regulated according to environmental O2 availability at the transcriptional level and that the concentration of cAMP in cells is regulated by DOS(Ec) expression
Title: DOS(Ec), a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli.
It appears that Leu99 and Leu115 are critical for determining the characteristics of heme iron. Finally, we discuss the roles of these amino-acid residues in the heme electronic states.
Title: Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables cyclic-guanylate-specific phosphodiesterase activity	IDA Inferred from Direct Assay more info	PubMed
enables cyclic-guanylate-specific phosphodiesterase activity	IEA Inferred from Electronic Annotation more info
enables heme binding	IDA Inferred from Direct Assay more info	PubMed
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxygen sensor activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in response to oxygen levels	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to oxygen levels	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to stimulus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: oxygen-sensing c-di-GMP phosphodiesterase DosP

NP_416006.4

EC 3.1.4.52

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

1563334..1565733 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_416006.4 oxygen-sensing c-di-GMP phosphodiesterase DosP [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_416006.4

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A376WYK1

Conserved Domains (1) summary

PRK11359
Location:1 → 799

PRK11359; cyclic-di-GMP phosphodiesterase; Provisional