| IED ID | IndEnz0002014464 |
| Enzyme Type ID | protease014464 |
| Protein Name |
Zinc metalloproteinase aureolysin EC 3.4.24.29 Staphylococcus aureus neutral proteinase |
| Gene Name | aur |
| Organism | Staphylococcus aureus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus |
| Enzyme Sequence | MRKFSRYAFTSMATVTLLSSLTPAALASDTNHKPATSDINFEITQKSDAVKALKELPKSENVKNHYQDYSVTDVKTDKKGFTHYTLQPSVDGVHAPDKEVKVHADKSGKVVLINGDTDAKKVKPTNKVTLSKDEAADKAFNAVKIDKNKAKNLQDDVIKENKVEIDGDSNKYIYNIELITVTPEISHWKVKIDADTGAVVEKTNLVKEAAATGTGKGVLGDTKDININSIDGGFSLEDLTHQGKLSAYNFNDQTGQATLITNEDENFVKDDQRAGVDANYYAKQTYDYYKNTFGRESYDNHGSPIVSLTHVNHYGGQDNRNNAAWIGDKMIYGDGDGRTFTNLSGANDVVAHELTHGVTQETANLEYKDQSGALNESFSDVFGYFVDDEDFLMGEDVYTPGKEGDALRSMSNPEQFGQPSHMKDYVYTEKDNGGVHTNSGIPNKAAYNVIQAIGKSKSEQIYYRALTEYLTSNSNFKDCKDALYQAAKDLYDEQTAEQVYEAWNEVGVE |
| Enzyme Length | 509 |
| Uniprot Accession Number | P81177 |
| Absorption | |
| Active Site | ACT_SITE 353; /evidence=ECO:0000305|PubMed:9753696; ACT_SITE 436; /note=Proton donor |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus.; EC=3.4.24.29; Evidence={ECO:0000269|PubMed:17878159}; |
| DNA Binding | |
| EC Number | 3.4.24.29 |
| Enzyme Function | FUNCTION: Plays an essential role in immune evasion by helping bacteria to resist complement-mediated killing by neutrophils. Inhibits the deposition of host C3b on bacterial surfaces and the release of the chemoattractant C5a by cleaving the central complement protein C3. The cleavage site renders the C3b molecule vulnerable to proteolytic degradation by host regulators (PubMed:21502375). Cleaves and inactivates host SERPINA1, which is an endogenous protease inhibitor essential for controlling neutrophil serine protease elastase (PubMed:3533918). Plays also an essential role in the cleavage and subsequent activation of the serine protease SspA (glutamyl endopeptidase) which is involved in colonization and infection of human tissues (PubMed:17878159). {ECO:0000269|PubMed:17878159, ECO:0000269|PubMed:21502375, ECO:0000269|PubMed:3533918}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (13); Chain (1); Helix (12); Metal binding (16); Propeptide (1); Sequence conflict (4); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1BQB; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,321 |
| Kinetics | |
| Metal Binding | METAL 348; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 352; /note="Zinc; catalytic; via tele nitrogen"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 356; /note="Zinc; catalytic; via tele nitrogen"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 376; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 387; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 387; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 389; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 390; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 390; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 392; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 395; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 395; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 398; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 399; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 402; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB"; METAL 405; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:9753696, ECO:0007744|PDB:1BQB" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.29; |