| IED ID | IndEnz0002008935 |
| Enzyme Type ID | protease008935 |
| Protein Name |
Signal peptidase complex catalytic subunit SEC11 PfSPC21 EC 3.4.21.89 Signal peptidase 21 kDa PfSP21 |
| Gene Name | SEC11 SPC21 PF3D7_1331300 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MDFIKEQYNSLVLDLRKTFRNKRDGLSHILNVICLLLNALMIWKLLVVFTGCESPVVVVLSGSMEPGYYRGDTLALYHPPKIHAGDVVVYQINGRDIPIVHRILSLHTSKDNKFHLLSKGDNNNIDDRGLYDPHQYWLENEHVLGLSVGYTPYIGILTIWINEYPVVKWAIVSIMLIMILMGYE |
| Enzyme Length | 184 |
| Uniprot Accession Number | Q8IE14 |
| Absorption | |
| Active Site | ACT_SITE 63; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P67812; ACT_SITE 101; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P67812; ACT_SITE 127; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P67812 |
| Activity Regulation | ACTIVITY REGULATION: Phosphorylation increases catalytic activity (PubMed:18054093). Ca(2+) slightly increases catalytic activity in vitro (PubMed:18054093). {ECO:0000269|PubMed:18054093}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000269|PubMed:18054093}; |
| DNA Binding | |
| EC Number | 3.4.21.89 |
| Enzyme Function | FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:18054093, PubMed:30127496). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity). {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:18054093, ECO:0000269|PubMed:30127496}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) |
| Keywords | Endoplasmic reticulum;Hydrolase;Membrane;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18054093, ECO:0000269|PubMed:30127496}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P13679}. Note=Partially colocalizes with SPC25 in the endoplasmic reticulum. {ECO:0000269|PubMed:30127496}. |
| Modified Residue | |
| Post Translational Modification | PTM: Phosphorylated (PubMed:18054093). Phosphorylation increases catalytic activity (PubMed:18054093). {ECO:0000269|PubMed:18054093}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,125 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |