| IED ID | IndEnz0002012497 |
| Enzyme Type ID | protease012497 |
| Protein Name |
Zinc metalloprotease MJ0392 EC 3.4.24.- MjS2P S2P endopeptidase Site-2-type intramembrane protease |
| Gene Name | MJ0392 |
| Organism | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Methanomada group Methanococci Methanococcales Methanocaldococcaceae Methanocaldococcus Methanocaldococcus jannaschii Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
| Enzyme Sequence | MNYSIRLFKIMGIPIELHITFILFLVVIIGLSIMNNSIFWAVLFILLFVSVVLHELGHSYVAKKYGVKIEKILLLPIGGVAMMDKIPKEGELRIGIAGPLVSFIIGIVLLIVSQFFDININGYPLLYTLSLLNLMLGGFNLIPAFPMDGGRILRAILSKKYGYLKSTKIAANIGKSLALIMLLFGLLSMNIILILVSLFVYFGAEQESRVVEVETIFKNIKAKDIMTPNPVYVTPDMSIEEFLDFMLKHKYFGYPVVENGKLVGCIGIGNIHKKEGTVRDYMEKPVVVSEDTDIKEILRKMANTDRVFVVEGGKLKGIISKTDILRAMSILELKEELKD |
| Enzyme Length | 339 |
| Uniprot Accession Number | Q57837 |
| Absorption | |
| Active Site | ACT_SITE 55; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:18063795" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000269|PubMed:18063795}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains; its endogenous substrate is unknown. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein. Possible signals, S1P and substrates are unknown in this organism. {ECO:0000269|PubMed:18063795}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Chain (1); Domain (2); Helix (7); Metal binding (3); Transmembrane (6) |
| Keywords | 3D-structure;CBS domain;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3B4R; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,965 |
| Kinetics | |
| Metal Binding | METAL 54; /note=Zinc; catalytic; METAL 58; /note=Zinc; catalytic; METAL 148; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.85; |