P0C0V0 · DEGP_ECOLI
- ProteinPeriplasmic serine endoprotease DegP
- GenedegP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814).
Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867).
DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688).
Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688).
Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477).
It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688).
DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP)
Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867).
DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688).
Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688).
Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477).
It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688).
DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP)
Miscellaneous
DegP is indispensable for bacterial survival at temperatures above 42 degrees Celsius, however is also able to digest its natural substrates in a reducing environment at temperatures as low as 20 degrees Celsius.
Catalytic activity
Activity regulation
Inhibited by diisopropylfluorophosphate (DFP).
Temperature Dependence
Optimum temperature is around 55 degrees Celsius. In the range from 37 to 55 degrees Celsius, the proteolytic activity rapidly increases with temperature.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 58 | substrate | ||||
Sequence: E | ||||||
Active site | 131 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 131 | substrate | ||||
Sequence: H | ||||||
Active site | 161 | Charge relay system | ||||
Sequence: D | ||||||
Binding site | 161 | substrate | ||||
Sequence: D | ||||||
Binding site | 234-236 | substrate | ||||
Sequence: GNS | ||||||
Active site | 236 | Charge relay system | ||||
Sequence: S | ||||||
Binding site | 252-256 | substrate | ||||
Sequence: TAILA | ||||||
Binding site | 291-295 | substrate | ||||
Sequence: LGIMG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Cellular Component | periplasmic space | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Molecular Function | peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | serine-type peptidase activity | |
Biological Process | chaperone-mediated protein folding | |
Biological Process | protein folding | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins | |
Biological Process | proteolysis | |
Biological Process | response to heat | |
Biological Process | response to oxidative stress | |
Biological Process | response to temperature stimulus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeriplasmic serine endoprotease DegP
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0C0V0
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Decreased induction of Cpx two-component regulatory system (PubMed:16166523).
Increased accumulation of periplasmic accessory protein CpxP, increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867).
Increased resistance to hydroxyurea, probably due to decreased degradation of misfolded proteins which eventually leads to decreased OH radical formation (PubMed:20005847).
Increased accumulation of periplasmic accessory protein CpxP, increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867).
Increased resistance to hydroxyurea, probably due to decreased degradation of misfolded proteins which eventually leads to decreased OH radical formation (PubMed:20005847).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 131 | Loss of peptidase activity with no detectable changes in secondary structure. | ||||
Sequence: H → R | ||||||
Mutagenesis | 236 | Loss of peptidase activity with no detectable changes in secondary structure. | ||||
Sequence: S → A | ||||||
Mutagenesis | 254 | It does not affect the proteolytic activity. | ||||
Sequence: I → N | ||||||
Mutagenesis | 255 | Loss of proteolytic activity. | ||||
Sequence: L → N | ||||||
Mutagenesis | 258 | Increases the proteolytic activity. | ||||
Sequence: D → V | ||||||
Mutagenesis | 261 | Loss of proteolytic activity. | ||||
Sequence: N → I | ||||||
Mutagenesis | 262 | Stimulates the proteolytic activity at low temperatures (20-30 degrees Celsius), whereas at higher temperatures (above 35 degrees Celsius), the proteolytic activity is less efficient. | ||||
Sequence: I → N | ||||||
Mutagenesis | 264 | Loss of proteolytic activity. | ||||
Sequence: I → N |
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MKKTTLALSALALSLGLALSPLSATA | ||||||
Chain | PRO_0000026921 | 27-474 | Periplasmic serine endoprotease DegP | |||
Sequence: AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ | ||||||
Disulfide bond | 83↔95 | |||||
Sequence: CQEGSPFQSSPFC |
Keywords
- PTM
Proteomic databases
Interaction
Subunit
DegP can reversibly switch between different oligomeric forms that represent inactive (6-mer) and active (12- and 24-mer) protease states. Substrate binding triggers the conversion of the resting DegP trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or 24-mer (DegP24) is crucial in regulating protease activity.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P0C0V0 | CSN2 P02666 | 9 | EBI-547165, EBI-5260183 | |
BINARY | P0C0V0 | degP P0C0V0 | 16 | EBI-547165, EBI-547165 | |
XENO | P0C0V0 | LYZ P00698 | 11 | EBI-547165, EBI-1029543 | |
BINARY | P0C0V0 | ompA P0A910 | 8 | EBI-547165, EBI-371347 | |
BINARY | P0C0V0 | ompC P06996 | 7 | EBI-547165, EBI-371155 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 280-371 | PDZ 1 | ||||
Sequence: MVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDG | ||||||
Domain | 377-466 | PDZ 2 | ||||
Sequence: NLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGD |
Sequence similarities
Belongs to the peptidase S1C family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length474
- Mass (Da)49,354
- Last updated2005-12-20 v1
- Checksum5482E596F74B6D5F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10 | in Ref. 1; AAA23994 and 7; AAA23680 | ||||
Sequence: A → R | ||||||
Sequence conflict | 46 | in Ref. 6; AAA23717 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 192 | in Ref. 1; AAA23994/CAA30997 | ||||
Sequence: A → G | ||||||
Sequence conflict | 467-474 | in Ref. 1; AAA23994/CAA30997 | ||||
Sequence: STIYLLMQ → RHLPVNAVISLNPFLKTGRGSPYNL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M36536 EMBL· GenBank· DDBJ | AAA23994.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X12457 EMBL· GenBank· DDBJ | CAA30997.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U70214 EMBL· GenBank· DDBJ | AAB08591.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73272.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAB96738.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29955 EMBL· GenBank· DDBJ | AAA23717.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M31772 EMBL· GenBank· DDBJ | AAA23680.1 EMBL· GenBank· DDBJ | Genomic DNA |