| IED ID | IndEnz0002009167 |
| Enzyme Type ID | protease009167 |
| Protein Name |
Serine protease 1 EC 3.4.21.- Serine protease I RPI |
| Gene Name | |
| Organism | Rarobacter faecitabidus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Rarobacteraceae Rarobacter Rarobacter faecitabidus |
| Enzyme Sequence | MKCKKPSALFSALALVGALGAASVLGAASANSASPVAAATVQASSGSAKTSVAATSKSQDGDVLAAIVRDLKITKTQAKKRIKLEEKARQLEPRLQKKLGKKFAGLWISKNGKKIVVGVTTKKAAKVVKKAGATPKIVKSNLTTLKKRATKISKNAPSDIKNVNSWWVDPATNKVVIEARSKKAAKAAATAAGLTAGTYEITVSDDVIVPVRDYWGGDALSGCTLAFPVYGGFLTAGHCAVEGKGHILKTEMTGGQIGTVEASQFGDGIDAAWAKNYGDWNGRGRVTHWNGGGGVDIKGSNEAAVGAHMCKSGRTTKWTCGYLLRKDVSVNYGNGHIVTLNETSACALGGDSGGAYVWNDQAQGITSGSNMDTNNCRSFYQPVNTVLNKWKLSLVTSTDVTTSYVQGYQNNCIDVPNSDFTDGKQLQVWNCNGTNAQKVSFHPDGTLRINGKCLDARWAWTHNGTEVQLMNCNGHIAQKFTLNGAGDLVNVHANKCVDVKDWGGQGGKLQLWECSGGANQKWWRR |
| Enzyme Length | 525 |
| Uniprot Accession Number | Q05308 |
| Absorption | |
| Active Site | ACT_SITE 238; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 270; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 352; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Major serine protease exhibiting lytic activity toward living yeast cells. Similar to elastase in its substrate specificity and has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Lectin;Mannose-binding;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,654 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |