| IED ID | IndEnz0002009453 |
| Enzyme Type ID | protease009453 |
| Protein Name |
Thermophilic serine proteinase EC 3.4.21.- Ak.1 protease |
| Gene Name | |
| Organism | Bacillus sp. (strain AK1) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain AK1) |
| Enzyme Sequence | MKFKAIVSLSLAVSMSLFPFLVEAASNDGVESPKTVSEINVSHEKGAYVQGEVIVQFKEQVNAEEKAKALKEVGATAVPDNDRVKSKFNVLKVGNVEAVVKALNNNPLVEYAEPNYLFNAAWTPNDTYYQGYQYGPQNTYTDYAWDVTKGSSGQEIAVIDTGVDYTHPDLDGKVIKGYDFVDNDYDPMDLNNHGTHVAGIAAAETNNATGIAGMAPNTRILAVRALDRNGSGTLSDIADAIIYAADSGAEVINLSLGCDCHTTTLENAVNYAWNKGSVVVAAAGNNGSSTTFEPASYENVIAVGAVDQYDRLASFSNYGTWVDVVAPGVDIVSTITGNRYAYMSGTSMASPHVAGLAALLASQGRNNIEIRQAIEQTADKISGTGTYFKYGRINSYNAVTY |
| Enzyme Length | 401 |
| Uniprot Accession Number | Q45670 |
| Absorption | |
| Active Site | ACT_SITE 160; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:10588904"; ACT_SITE 193; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:10588904"; ACT_SITE 347; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:10588904" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Helix (9); Metal binding (15); Propeptide (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Signal;Sodium;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1DBI; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,835 |
| Kinetics | |
| Metal Binding | METAL 126; /note=Calcium 1; /evidence=ECO:0000269|PubMed:10588904; METAL 168; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 169; /note=Calcium 1; /evidence=ECO:0000269|PubMed:10588904; METAL 171; /note=Calcium 3; /evidence=ECO:0000269|PubMed:10588904; METAL 179; /note=Calcium 2; /evidence=ECO:0000269|PubMed:10588904; METAL 184; /note=Calcium 2; /evidence=ECO:0000269|PubMed:10588904; METAL 186; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 204; /note=Calcium 1; /evidence=ECO:0000269|PubMed:10588904; METAL 204; /note=Calcium 3; /evidence=ECO:0000269|PubMed:10588904; METAL 207; /note=Calcium 1; /evidence=ECO:0000269|PubMed:10588904; METAL 209; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 211; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 297; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 300; /note=Sodium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:10588904; METAL 323; /note=Sodium; /evidence=ECO:0000269|PubMed:10588904 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.62; |