degP [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: 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_000913.3 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?

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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

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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 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	IBA Inferred from Biological aspect of Ancestor more info
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

EC 3.4.21.107

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

180884..182308

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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