| IED ID | IndEnz0009000036 |
| Enzyme Type ID | chitinase000036 |
| Protein Name |
Protease 1 EC 3.4.21.50 API Lysyl endopeptidase Protease I |
| Gene Name | |
| Organism | Achromobacter lyticus |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Alcaligenaceae Achromobacter Achromobacter lyticus |
| Enzyme Sequence | MKRICGSLLLLGLSISAALAAPASRPAAFDYANLSSVDKVALRTMPAVDVAKAKAEDLQRDKRGDIPRFALAIDVDMTPQNSGAWEYTADGQFAVWRQRVRSEKALSLNFGFTDYYMPAGGRLLVYPATQAPAGDRGLISQYDASNNNSARQLWTAVVPGAEAVIEAVIPRDKVGEFKLRLTKVNHDYVGFGPLARRLAAASGEKGVSGSCNIDVVCPEGDGRRDIIRAVGAYSKSGTLACTGSLVNNTANDRKMYFLTAHHCGMGTASTAASIVVYWNYQNSTCRAPNTPASGANGDGSMSQTQSGSTVKATYATSDFTLLELNNAANPAFNLFWAGWDRRDQNYPGAIAIHHPNVAEKRISNSTSPTSFVAWGGGAGTTHLNVQWQPSGGVTEPGSSGSPIYSPEKRVLGQLHGGPSSCSATGTNRSDQYGRVFTSWTGGGAAASRLSDWLDPASTGAQFIDGLDSGGGTPNTPPVANFTSTTSGLTATFTDSSTDSDGSIASRSWNFGDGSTSTATNPSKTYAAAGTYTVTLTVTDNGGATNTKTGSVTVSGGPGAQTYTNDTDVAIPDNATVESPITVSGRTGNGSATTPIQVTIYHTYKSDLKVDLVAPDGTVYNLHNRTGGSAHNIIQTFTKDLSSEAAQRAPGSCG |
| Enzyme Length | 653 |
| Uniprot Accession Number | P15636 |
| Absorption | |
| Active Site | ACT_SITE 262; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 318; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 399; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.; EC=3.4.21.50; |
| DNA Binding | |
| EC Number | 3.4.21.50 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (17); Chain (1); Disulfide bond (3); Domain (2); Helix (11); Propeptide (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;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: Three disulfide bonds are present. {ECO:0000269|PubMed:2492988}. |
| Signal Peptide | SIGNAL 1..20; /note=Or 27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1ARB; 1ARC; 4GPG; |
| Mapped Pubmed ID | 23714114; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,125 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.50; |