| IED ID | IndEnz0002005100 |
| Enzyme Type ID | protease005100 |
| Protein Name |
Aqualysin-1 EC 3.4.21.111 Aqualysin-I |
| Gene Name | pstI |
| Organism | Thermus aquaticus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Thermus Thermus aquaticus |
| Enzyme Sequence | MRKTYWLMALFAVLVLGGCQMASRSDPTPTLAEAFWPKEAPVYGLDDPEAIPGRYIVVFKKGKGQSLLQGGITTLQARLAPQGVVVTQAYTGALQGFAAEMAPQALEAFRQSPDVEFIEADKVVRAWATQSPAPWGLDRIDQRDLPLSNSYTYTATGRGVNVYVIDTGIRTTHREFGGRARVGYDALGGNGQDCNGHGTHVAGTIGGVTYGVAKAVNLYAVRVLDCNGSGSTSGVIAGVDWVTRNHRRPAVANMSLGGGVSTALDNAVKNSIAAGVVYAVAAGNDNANACNYSPARVAEALTVGATTSSDARASFSNYGSCVDLFAPGASIPSAWYTSDTATQTLNGTSMATPHVAGVAALYLEQNPSATPASVASAILNGATTGRLSGIGSGSPNRLLYSLLSSGSGSTAPCTSCSYYTGSLSGPGDYNFQPNGTYYYSPAGTHRAWLRGPAGTDFDLYLWRWDGSRWLTVGSSTGPTSEESLSYSGTAGYYLWRIYAYSGSGMYEFWLQRP |
| Enzyme Length | 513 |
| Uniprot Accession Number | P08594 |
| Absorption | |
| Active Site | ACT_SITE 166; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 197; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 349; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.; EC=3.4.21.111; |
| DNA Binding | |
| EC Number | 3.4.21.111 |
| Enzyme Function | FUNCTION: Aqualysin I is a thermophilic alkaline serine protease. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius for caseinolytic activity.; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Chain (1); Disulfide bond (2); Domain (2); Helix (8); Propeptide (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N- and C-terminal Pro-sequences are successively removed through the proteolytic activity of PstI itself. The C-terminal Pro-sequence is required for translocation of the proteases across the outer membrane. |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000269|PubMed:2182621 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4DZT; |
| Mapped Pubmed ID | 15299524; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,913 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.111; |