| IED ID | IndEnz0002009901 |
| Enzyme Type ID | protease009901 |
| Protein Name |
Secreted aspartyl protease 1 EC 3.4.23.- |
| Gene Name | SAP1 MGL_1932 |
| Organism | Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Malasseziomycetes Malasseziales Malasseziaceae Malassezia Malassezia globosa Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus) |
| Enzyme Sequence | MQLSIQAIIGFVVAAGLAVASELPSPMTVNLERRKMLVTKNDTVDFKAVRKQANALNYKYDKLLRNFRKNTGRDHPLLHLLLDLIDKRDGKGDVDLDDIGEGQLWAGDVQFGQSKFKIDFDTGSADTLVNPFVYFPHRSKSSRKTHHTFSTAYGDGTTASGFIYTDDLKIGGYKAKDVAIGLSVTKFINDEDNQGIAGMSFPAVQSFPKKFDPFFVALVKQKVVPEPVFQFTLKRGSGSTLHLGGIDNSRFQGELSYVDVNPEDGFWISEGKVNGKKIDACIDTGSSIIFGPIDEVREVITKMDGVTPFTAGGALHGAFDCSKPPKLDFEFAGQKFNLGENQVSFGKYQGQCVLSIMGQKNLPMNAWVVGDSFLQTASVVFDMGKNRMGFAPSSN |
| Enzyme Length | 395 |
| Uniprot Accession Number | A8PZM4 |
| Absorption | |
| Active Site | ACT_SITE 121; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 283; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin A. {ECO:0000269|PubMed:29246799}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Dominant secreted aspartyl protease that has a clear preference for aromatic residues in the P1' position directly adjacent to the cleavage site and, in particular, Trp. In addition, it generally cleaves peptides containing Lys, Arg, Phe, Tyr, or Nle (norleucine) in the P1 position, Nle and Glu at P2, and Arg and Val at P2'. Has important roles in facilitating the interaction of the yeast with the external environment (PubMed:29246799). Is able to rapidly hydrolyze Staphylococcus aureus protein A, an important S.aureus virulence factor involved in immune evasion and biofilm formation. Shows anti-biofilm properties and thus plays a role in inter-kingdom interactions, beneficial for host skin health (PubMed:29246799). {ECO:0000269|PubMed:29246799}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Highly expressed during exponential growth in rich media (PubMed:29246799). Also part of the 3 most highly expressed extracellular proteases in minimal media (PubMed:29246799). Expressed on human skin (PubMed:29246799). {ECO:0000269|PubMed:29246799}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29246799}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,273 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for peptide RPKPVE-Nva-WRK {ECO:0000269|PubMed:29246799}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |