UniProt functional annotation for P39099



	UniProt functional annotation for P39099

UniProt code: P39099.

Organism: Escherichia coli (strain K12).

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

Function: DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP. {ECO:0000269|PubMed:8576051, 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;

Activity regulation: Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269|PubMed:8576051}.

Biophysicochemical properties: pH dependence: Optimum pH is 5.5. The degradation is efficient at pH values between 4.5 and 6. {ECO:0000269|PubMed:21685389};

Subunit: DegQ 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 DegQ trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegQ6) into 12-mer (DegQ12) or 24-mer (DegQ24) is crucial in regulating protease activity. {ECO:0000269|PubMed:21685389, ECO:0000269|PubMed:8830688}.

Subcellular location: Periplasm {ECO:0000269|PubMed:8576051}.

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:		DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP. {ECO:0000269\|PubMed:8576051, 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;
Activity regulation:		Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269\|PubMed:8576051}.
Biophysicochemical properties:		pH dependence: Optimum pH is 5.5. The degradation is efficient at pH values between 4.5 and 6. {ECO:0000269\|PubMed:21685389};
Subunit:		DegQ 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 DegQ trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegQ6) into 12-mer (DegQ12) or 24-mer (DegQ24) is crucial in regulating protease activity. {ECO:0000269\|PubMed:21685389, ECO:0000269\|PubMed:8830688}.
Subcellular location:		Periplasm {ECO:0000269\|PubMed:8576051}.
Similarity:		Belongs to the peptidase S1C family. {ECO:0000305}.