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    degP periplasmic serine endoprotease DegP [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947139, updated on 17-Dec-2024

    Summary

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    Official Symbol
    degP
    Official Full Name
    periplasmic serine endoprotease DegP
    Primary source
    ECOCYC:EG10463
    Locus tag
    b0161
    See related
    ASAP:ABE-0000551
    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
    ECK0160; htrA; ptd
    Summary
    Autocleavage occurs after Cys95(Cys69 of mature form) or Gln108 (Gln82 of mature form). [More information is available at EcoGene: EG10463]. Protease Do, or DegP, is a periplasmic serine protease required for survival at high temperatures . [More information is available at EcoCyc: EG10463].
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    Genomic context

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    Sequence:
    NC_000913.3 (180884..182308)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene vitamin B12 ABC transporter periplasmic binding protein Neighboring gene 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Neighboring gene dGTP triphosphohydrolase Neighboring gene DNA-binding transcriptional activator CdaR Neighboring gene DUF3461 domain-containing protein YaeH

    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. The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Skórko-Glonek J, et al. Mol Gen Genet, 1999 Sep. PMID 10517331
    2. Temperature-induced conformational changes within the regulatory loops L1-L2-LA of the HtrA heat-shock protease from Escherichia coli. Sobiecka-Szkatula A, et al. Biochim Biophys Acta, 2009 Nov. PMID 19615474
    3. Assemblies of DegP underlie its dual chaperone and protease function. Subrini O, et al. FEMS Microbiol Lett, 2009 Jun. PMID 19508278
    4. Escherichia coli DegP: a structure-driven functional model. Ortega J, et al. J Bacteriol, 2009 Aug. PMID 19465652, Free PMC Article
    5. Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Shen QT, et al. Proc Natl Acad Sci U S A, 2009 Mar 24. PMID 19255437, Free PMC Article

    See all (114) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.
      Title: Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.
    2. DegP plays a critical role in protein quality control in the bacterial periplasm by degrading both periplasmic proteins and beta-barrel outer membrane proteins under stress conditions and likely also by participating in the folding of chimeric beta-barrel outer membrane proteins.
      Title: Degp degrades a wide range of substrate proteins in Escherichia coli under stress conditions.
    3. Suppressor mutations in degS overcome the acute temperature-sensitive phenotype of DeltadegP and DeltadegP Deltatol-pal mutants of Escherichia coli.
      Title: Suppressor Mutations in degS Overcome the Acute Temperature-Sensitive Phenotype of ΔdegP and ΔdegP Δtol-pal Mutants of Escherichia coli.
    4. demonstrate the interaction of DegP with typical cellular substrate proteins in cells during acid stress and/or recovery stages by using unnatural amino acid-mediated in vivo photo-crosslinking, as well as the degradation of periplasmic proteins by DegP during recovery after acidic denaturation
      Title: DegP functions as a critical protease for bacterial acid resistance.
    5. Our results suggest that YjfN is a novel "suicide activator" for DegP that enhances DegP proteolysis under misfolded protein stress.
      Title: A Small Periplasmic Protein with a Hydrophobic C-Terminal Residue Enhances DegP Proteolysis as a Suicide Activator.
    6. Here, the authors demonstrate that a mutant variant of an outer-membrane lipoprotein, Lpp(+Leu), can function as a novel allosteric effector that changes the dynamic range of DegP activity.
      Title: Tripodal Lipoprotein Variants with C-Terminal Hydrophobic Residues Allosterically Modulate Activity of the DegP Protease.
    7. These results demonstrate that multiple periplasmic proteases monitor outer membrane proteins at distinct points in the assembly process as in the case of degradation of the outer membrane protein LptD by the DegP, BepA and YcaL proteases.
      Title: Distinctive Roles for Periplasmic Proteases in the Maintenance of Essential Outer Membrane Protein Assembly.
    8. Investigated the influence of amino acid substitutions located within the LD loop on the kinetics of a model substrate cleavage as well as on the dynamics of the oligomeric structure of HtrA. We found that the mutations that were expected to disturb the loop's structure and/or interactions with the remaining regulatory loops severely diminished the proteolytic activity of HtrA.
      Title: The LD loop as an important structural element required for transmission of the allosteric signal in the HtrA (DegP) protease from Escherichia coli.
    9. In the present review, we summarize recent advances in the characterization of these key factors, with a special emphasis on the multifunctional protein DegP.
      Title: Periplasmic quality control in biogenesis of outer membrane proteins.
    10. The lack of the disulfide within LA affected the stability and the overall structure of the HtrA molecule.
      Title: Analysis of the link between the redox state and enzymatic activity of the HtrA (DegP) protein from Escherichia coli.
    Submit: New GeneRIF Correction See all GeneRIFs (25)

    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 endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type peptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables serine-type peptidase activity ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within protein quality control for misfolded or incompletely synthesized proteins EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in protein quality control for misfolded or incompletely synthesized proteins IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within protein quality control for misfolded or incompletely synthesized proteins IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within protein quality control for misfolded or incompletely synthesized proteins IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proteolysis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within response to oxidative stress IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within response to temperature stimulus IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    periplasmic serine endoprotease DegP
    NP_414703.1

    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

    1. NC_000913.3 Reference assembly

      Range
      180884..182308
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414703.1 periplasmic serine endoprotease DegP [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414703.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A775UL22
      Conserved Domains (1) summary
      PRK10942
      Location:2 → 474
      PRK10942; serine endoprotease DegP
    Nucleotide Protein
    Heading Accession and Version

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