| IED ID | IndEnz0002001963 |
| Enzyme Type ID | protease001963 |
| Protein Name |
Membrane-bound protease PH1510 EC 3.4.21.- NfeD homolog Stomatin operon partner protein STOPP |
| Gene Name | PH1510 |
| Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus horikoshii Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Enzyme Sequence | MRRILLSMIVLIFLASPILAKNIVYVAQIKGQITSYTYDQFDRYITIAEQDNAEAIIIELDTPGGRADAMMNIVQRIQQSKIPVIIYVYPPGASAASAGTYIALGSHLIAMAPGTSIGACRPILGYSQNGSIIEAPPKITNYFIAYIKSLAQESGRNATIAEEFITKDLSLTPEEALKYGVIEVVARDINELLKKSNGMKTKIPVNGRYVTLNFTNVEVRYLAPSFKDKLISYITDPNVAYLLLTLGIWALIIGFLTPGWHVPETVGAIMIILAIIGFGYFGYNSAGILLIIVAMLFFIAEALTPTFGLFTVAGLITFIIGGILLFGGGEEYLVRKEVFSQLRILIITVGAILAAFFAFGMAAVIRAHKKKARTGKEEMIGLIGTVVEELNPEGMIKVRGELWKARSKFNGKIEKGEKVRVVDMDGLTLIVVRERKEGGEK |
| Enzyme Length | 441 |
| Uniprot Accession Number | O59179 |
| Absorption | |
| Active Site | ACT_SITE 97; /note=Nucleophile; ACT_SITE 138; /note=Proton donor/acceptor |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by divalent metal cations, including Mg(2+), Mn(2+), Ca(2+) and Zn(2+). Mildly inhibited by 0.01 % SDS and 0.1% dodecyl-beta-D-maltoside. Activity is nearly abolished by 1 % SDS. {ECO:0000269|PubMed:15611110}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro). {ECO:0000269|PubMed:15611110, ECO:0000269|PubMed:16574150, ECO:0000269|PubMed:24121343}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is above 90 degrees Celsius. {ECO:0000269|PubMed:15611110}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6. {ECO:0000269|PubMed:15611110}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Chain (1); Helix (9); Mutagenesis (4); Region (2); Signal peptide (1); Transmembrane (4) |
| Keywords | 3D-structure;Hydrolase;Membrane;Protease;Serine protease;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 2DEO; 3BPP; 3VIV; 3WG5; 3WWV; 6M4B; |
| Mapped Pubmed ID | 23587725; 25349784; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,281 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B56; |