Detail Information for IndEnz0002001794
IED ID IndEnz0002001794
Enzyme Type ID protease001794
Protein Name Subtilisin-like protease 2
EC 3.4.21.62
Merozoite surface sheddase
MESH
PfSUB2
Gene Name SUB2
Organism Plasmodium falciparum
Taxonomic Lineage cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum
Enzyme Sequence MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEEKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKIENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADIKHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLMKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK
Enzyme Length 1342
Uniprot Accession Number O97364
Absorption
Active Site ACT_SITE 755; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 798; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 961; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240
Activity Regulation ACTIVITY REGULATION: Activation may be calcium-dependent (PubMed:16322767). Inhibited by the non-covalent interaction with the cleaved propeptide (PubMed:16322767). {ECO:0000269|PubMed:16322767}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000305|PubMed:16322767};
DNA Binding
EC Number 3.4.21.62
Enzyme Function FUNCTION: Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite (PubMed:16322767). May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (By similarity). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:16322767}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (4); Chain (1); Compositional bias (3); Domain (1); Glycosylation (14); Helix (2); Propeptide (1); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1)
Keywords 3D-structure;Autocatalytic cleavage;Cell membrane;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Membrane;Protease;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10551362, PubMed:16322767). Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (PubMed:16322767). {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}.
Modified Residue
Post Translational Modification PTM: Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10551362, PubMed:16322767). The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity). The second cleavage may be mediated by PMX/plasmepsin X (By similarity). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2LU1;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 154,932
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda