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

    Gene ID: 945815, updated on 3-Dec-2024

    Summary

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    Official Symbol
    dosP
    Official Full Name
    oxygen-sensing c-di-GMP phosphodiesterase DosP
    Primary source
    ECOCYC:G6783
    Locus tag
    b1489
    See related
    ASAP:ABE-0004963
    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_000913.3Genomic Context describing neighboring genes Neighboring gene putative D,D-dipeptide ABC transporter periplasmic binding protein Neighboring gene D-alanyl-D-alanine dipeptidase Neighboring gene diguanylate cyclase DosC Neighboring gene protein YddY

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. Kurokawa H, et al. J Biol Chem, 2004 May 7. PMID 14982921
    2. A comparative resonance Raman analysis of heme-binding PAS domains: heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins. Tomita T, et al. Biochemistry, 2002 Apr 16. PMID 11939776
    3. DOS(Ec), a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli. Yoshimura-Suzuki T, et al. J Bacteriol, 2005 Oct. PMID 16166529, Free PMC Article
    4. Investigation of the relationship between protein-protein interaction and catalytic activity of a heme-regulated phosphodiesterase from Escherichia coli (Ec DOS) by protein microarray. Sasakura Y, et al. Biochemistry, 2005 Jul 19. PMID 16008345
    5. Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure. Sasakura Y, et al. J Biol Chem, 2002 Jun 28. PMID 11970957

    See all (50) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. 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.
    3. 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.
    4. 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.
    5. 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.
    6. 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.
    7. 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.
    8. 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.
    9. 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.
    10. 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.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    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 

    General protein information

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    Preferred Names
    oxygen-sensing c-di-GMP phosphodiesterase DosP
    NP_416006.4

    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

    1. NC_000913.3 Reference assembly

      Range
      1563334..1565733 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. 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
    Nucleotide Protein
    Heading Accession and Version

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