UniProt functional annotation for Q5JIZ5



	UniProt functional annotation for Q5JIZ5

UniProt code: Q5JIZ5.

Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)).

Taxonomy: Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Thermococcus.

Function: Serine protease with a broad substrate specificity. {ECO:0000269|PubMed:20100702}.

Catalytic activity: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:20100702};

Activity regulation: Resistant to treatment with 5% SDS, 8 M urea, 10% Triton X-100 or 10% Tween-20. Fully active although less stable in the presence of 10 mM EDTA. Activity not affected by the absence or presence of 10 mM CaCl(2). Unstable in the presence of 2 M or over GdnHCl and loses 35% and 99% of its activity upon incubation with 2 and 4 M GdnHCl, respectively, for 1 hour at 55 degrees Celsius. Nearly fully loses activity upon incubation at pH 2.0. {ECO:0000269|PubMed:20100702}.

Biophysicochemical properties: Kinetic parameters: KM=0.11 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.5 {ECO:0000269|PubMed:20100702}; KM=0.41 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.5 {ECO:0000269|PubMed:20100702}; Vmax=510 umol/min/mg enzyme {ECO:0000269|PubMed:20100702}; Note=Kcat is 1.6 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.5(PubMed:20100702). Kcat is 25 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.5(PubMed:20100702). {ECO:0000269|PubMed:20100702}; pH dependence: High activity at a wide pH range between 7.0-11.5 at 20 degrees Celsius and pH 7.5. It is not fully stable at pH 6 or under and at pH 12 or over. It loses over 85% of its activity at pH 3 or under and at pH 13. {ECO:0000269|PubMed:20100702}; Temperature dependence: Optimum temperature is about 100 degrees Celsius. Highly thermostable. Stable at 80 degrees Celsius for at least 3 hours. Half-life at 100 degrees Celsius is 100 minutes and at 90 degrees Celsius more than 3 hours. {ECO:0000269|PubMed:20100702};

Subunit: Monomer. {ECO:0000269|PubMed:20100702, ECO:0000269|PubMed:20595040}.

Domain: The C-terminal calcium-binding beta-jelly roll domain (445-562) of the mature domain is not required for folding or activity, but it is required for the hyperstabilization of the protein and possibly for its adaptation to high-temperature environment. {ECO:0000269|PubMed:20595040}.

Mass spectrometry: Mass=44187; Mass_error=202; Method=MALDI; Evidence={ECO:0000269|PubMed:20100702};

Biotechnology: Has potential for application in biotechnology fields due to its high resistance to heat, denaturants, detergents and chelating agents. {ECO:0000303|PubMed:20100702}.

Similarity: Belongs to the peptidase S8 family. {ECO:0000255|RuleBase:RU003355}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)).
Taxonomy:		Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Thermococcus.



Function:		Serine protease with a broad substrate specificity. {ECO:0000269\|PubMed:20100702}.


Catalytic activity:		Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269\|PubMed:20100702};
Activity regulation:		Resistant to treatment with 5% SDS, 8 M urea, 10% Triton X-100 or 10% Tween-20. Fully active although less stable in the presence of 10 mM EDTA. Activity not affected by the absence or presence of 10 mM CaCl(2). Unstable in the presence of 2 M or over GdnHCl and loses 35% and 99% of its activity upon incubation with 2 and 4 M GdnHCl, respectively, for 1 hour at 55 degrees Celsius. Nearly fully loses activity upon incubation at pH 2.0. {ECO:0000269\|PubMed:20100702}.
Biophysicochemical properties:		Kinetic parameters: KM=0.11 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.5 {ECO:0000269\|PubMed:20100702}; KM=0.41 mM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.5 {ECO:0000269\|PubMed:20100702}; Vmax=510 umol/min/mg enzyme {ECO:0000269\|PubMed:20100702}; Note=Kcat is 1.6 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.5(PubMed:20100702). Kcat is 25 s(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.5(PubMed:20100702). {ECO:0000269\|PubMed:20100702}; pH dependence: High activity at a wide pH range between 7.0-11.5 at 20 degrees Celsius and pH 7.5. It is not fully stable at pH 6 or under and at pH 12 or over. It loses over 85% of its activity at pH 3 or under and at pH 13. {ECO:0000269\|PubMed:20100702}; Temperature dependence: Optimum temperature is about 100 degrees Celsius. Highly thermostable. Stable at 80 degrees Celsius for at least 3 hours. Half-life at 100 degrees Celsius is 100 minutes and at 90 degrees Celsius more than 3 hours. {ECO:0000269\|PubMed:20100702};
Subunit:		Monomer. {ECO:0000269\|PubMed:20100702, ECO:0000269\|PubMed:20595040}.
Domain:		The C-terminal calcium-binding beta-jelly roll domain (445-562) of the mature domain is not required for folding or activity, but it is required for the hyperstabilization of the protein and possibly for its adaptation to high-temperature environment. {ECO:0000269\|PubMed:20595040}.
Mass spectrometry:		Mass=44187; Mass_error=202; Method=MALDI; Evidence={ECO:0000269\|PubMed:20100702};
Biotechnology:		Has potential for application in biotechnology fields due to its high resistance to heat, denaturants, detergents and chelating agents. {ECO:0000303\|PubMed:20100702}.
Similarity:		Belongs to the peptidase S8 family. {ECO:0000255\|RuleBase:RU003355}.