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

Gene ID: 947139, updated on 4-Feb-2026
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
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
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 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 periplasmic space IEA
Inferred from Electronic Annotation
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
  
Preferred Names
periplasmic serine endoprotease DegP
NP_414703.1

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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

    See identical proteins and their annotated locations for NP_414703.1

    Status: REVIEWED

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