| IED ID | IndEnz0002011019 |
| Enzyme Type ID | protease011019 |
| Protein Name |
Subtilisin-like serine protease EC 3.4.21.62 Tk-SP |
| Gene Name | TK1689 |
| Organism | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus kodakarensis Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Enzyme Sequence | MKKFGAVVLALFLVGLMAGSVLAAPQKPAVRNVSQQKNYGLLTPGLFKKVQRMSWDQEVSTIIMFDNQADKEKAVEILDFLGAKIKYNYHIIPALAVKIKVKDLLIIAGLMDTGYFGNAQLSGVQFIQEDYVVKVAVETEGLDESAAQVMATNMWNLGYDGSGITIGIIDTGIDASHPDLQGKVIGWVDFVNGKTTPYDDNGHGTHVASIAAGTGAASNGKYKGMAPGAKLVGIKVLNGQGSGSISDIINGVDWAVQNKDKYGIKVINLSLGSSQSSDGTDSLSQAVNNAWDAGLVVVVAAGNSGPNKYTVGSPAAASKVITVGAVDKYDVITDFSSRGPTADNRLKPEVVAPGNWIIAARASGTSMGQPINDYYTAAPGTSMATPHVAGIAALLLQAHPSWTPDKVKTALIETADIVKPDEIADIAYGAGRVNAYKAAYYDNYAKLTFTGYVSNKGSQSHQFTISGAGFVTATLYWDNSGSDLDLYLYDPNGNQVDYSYTAYYGFEKVGYYNPTAGTWTIKVVSYSGSANYQVDVVSDGSLGQPSGGGSEPSPSPSPEPTVDEKTFTGTVHDYYDKSDTFTMTVNSGATKITGDLYFDTSYHDLDLYLYDPNQNLVDRSESSNSYEHVEYNNPAPGTWYFLVYAYDTYGYADYQLDAKVYYG |
| Enzyme Length | 663 |
| Uniprot Accession Number | Q5JIZ5 |
| Absorption | |
| Active Site | ACT_SITE 170; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20595040"; ACT_SITE 203; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20595040"; ACT_SITE 382; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20595040" |
| Activity Regulation | 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}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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}; |
| DNA Binding | |
| EC Number | 3.4.21.62 |
| Enzyme Function | FUNCTION: Serine protease with a broad substrate specificity. {ECO:0000269|PubMed:20100702}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: 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}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: 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}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (28); Chain (1); Domain (1); Helix (14); Metal binding (9); Mutagenesis (2); Propeptide (2); Region (1); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:20595040 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3AFG; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,955 |
| Kinetics | 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 sec(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 20 degrees Celsius and pH 7.5(PubMed:20100702). kcat is 25 sec(-1) for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide at 80 degrees Celsius and pH 7.5(PubMed:20100702). {ECO:0000269|PubMed:20100702}; |
| Metal Binding | METAL 420; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20595040; METAL 423; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20595040; METAL 483; /note=Calcium 2; /evidence=ECO:0000269|PubMed:20595040; METAL 484; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20595040; METAL 485; /note=Calcium 2; /evidence=ECO:0000269|PubMed:20595040; METAL 497; /note=Calcium 1; /evidence=ECO:0000269|PubMed:20595040; METAL 498; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20595040; METAL 501; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20595040; METAL 507; /note=Calcium 2; /evidence=ECO:0000269|PubMed:20595040 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.62; |