| IED ID | IndEnz0002013189 |
| Enzyme Type ID | protease013189 |
| Protein Name |
Ulilysin EC 3.4.24.- |
| Gene Name | MA_3214 |
| Organism | Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Methanomicrobia Methanosarcinales Methanosarcinaceae Methanosarcina Methanosarcina acetivorans Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
| Enzyme Sequence | MAEKFESRGIEEASSEVPTQRRCGAMEVHHRLLRSASYVRERDQIENLALKYKQGFRAISRMEIVKIPVVVHVVWNEEEENISDAQIQSQIDILNKDFRKLNSDVSQVPSVWSNLIADLGIEFFLATKDPNGNQTTGITRTQTSVTFFTTSDEVKFASSGGEDAWPADRYLNIWVCHVLKSEIGQDILGYAQFPGGPAETDGVVIVDAAFGTTGTALPPFDKGRTATHEIGHWLNLYHIWGDELRFEDPCSRSDEVDDTPNQADPNFGCPSYPHVSCSNGPNGDMFMNYMDYVDDKCMVMFTQGQATRVNACLDGPRSSFLARVEETEKKEAPSKREMPMPR |
| Enzyme Length | 342 |
| Uniprot Accession Number | Q8TL28 |
| Absorption | |
| Active Site | ACT_SITE 229; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, excess zinc, and also significantly by batimastat in vitro. Is not inhibited by other metalloprotease inhibitors like phosphoramidon, captopril and galardine or those targeting other classes of proteases. {ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044}. |
| Binding Site | BINDING 225; /note=Substrate; /evidence=ECO:0000269|PubMed:16627477; BINDING 295; /note=Substrate; /evidence=ECO:0000269|PubMed:16627477 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond. {ECO:0000269|PubMed:16627477}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|Ref.3}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Binding site (2); Chain (1); Disulfide bond (2); Helix (11); Metal binding (11); Propeptide (2); Region (3); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The inactive zymogen pro-ulilysin undergoes calcium-mediated autolytic activation to the mature ulilysin. Autoproteolytic activation entails removal of the first 60 residues and of a highly charged 20-residue C-terminal tail. |
| Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2CKI; 2J83; 3LUM; 3LUN; |
| Mapped Pubmed ID | 20202937; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,371 |
| Kinetics | |
| Metal Binding | METAL 228; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 232; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 238; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 240; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 243; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 249; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 254; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 256; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 259; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 262; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044"; METAL 263; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16627477, ECO:0000269|PubMed:17097044" |
| Rhea ID | |
| Cross Reference Brenda |