Detail Information for IndEnz0002001963
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;