UniProt functional annotation for P0C0V0



	UniProt functional annotation for P0C0V0

UniProt code: P0C0V0.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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). {ECO:0000269|PubMed:10319814, ECO:0000269|PubMed:12730160, ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:18496527, ECO:0000269|PubMed:18505836, ECO:0000269|PubMed:2180903, ECO:0000269|PubMed:7557477, ECO:0000269|PubMed:8830688}.

Catalytic activity: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; Evidence={ECO:0000269|PubMed:8830688};

Activity regulation: Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269|PubMed:2180903}.

Biophysicochemical properties: 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. {ECO:0000269|PubMed:7744744};

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. {ECO:0000269|PubMed:11919638, ECO:0000269|PubMed:18496527, ECO:0000269|PubMed:18697939, ECO:0000269|PubMed:20581825, ECO:0000269|PubMed:21458668, ECO:0000269|PubMed:21526129, ECO:0000269|PubMed:8830688}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:9083020}; Peripheral membrane protein {ECO:0000269|PubMed:9083020}; Cytoplasmic side {ECO:0000269|PubMed:9083020}.

Induction: By heat shock (PubMed:3057437). Transcriptionally up- regulated by sigma-E factor and the Cpx two-component signal transduction pathway (PubMed:7883164, PubMed:9351822). {ECO:0000269|PubMed:3057437, ECO:0000269|PubMed:7883164, ECO:0000269|PubMed:9351822}.

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). {ECO:0000269|PubMed:16166523, ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:20005847}.

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.

Similarity: Belongs to the peptidase S1C family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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). {ECO:0000269\|PubMed:10319814, ECO:0000269\|PubMed:12730160, ECO:0000269\|PubMed:16303867, ECO:0000269\|PubMed:18496527, ECO:0000269\|PubMed:18505836, ECO:0000269\|PubMed:2180903, ECO:0000269\|PubMed:7557477, ECO:0000269\|PubMed:8830688}.


Catalytic activity:		Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-\|-Val.; EC=3.4.21.107; Evidence={ECO:0000269\|PubMed:8830688};
Activity regulation:		Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269\|PubMed:2180903}.
Biophysicochemical properties:		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. {ECO:0000269\|PubMed:7744744};
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. {ECO:0000269\|PubMed:11919638, ECO:0000269\|PubMed:18496527, ECO:0000269\|PubMed:18697939, ECO:0000269\|PubMed:20581825, ECO:0000269\|PubMed:21458668, ECO:0000269\|PubMed:21526129, ECO:0000269\|PubMed:8830688}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:9083020}; Peripheral membrane protein {ECO:0000269\|PubMed:9083020}; Cytoplasmic side {ECO:0000269\|PubMed:9083020}.
Induction:		By heat shock (PubMed:3057437). Transcriptionally up- regulated by sigma-E factor and the Cpx two-component signal transduction pathway (PubMed:7883164, PubMed:9351822). {ECO:0000269\|PubMed:3057437, ECO:0000269\|PubMed:7883164, ECO:0000269\|PubMed:9351822}.
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). {ECO:0000269\|PubMed:16166523, ECO:0000269\|PubMed:16303867, ECO:0000269\|PubMed:20005847}.
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.
Similarity:		Belongs to the peptidase S1C family. {ECO:0000305}.