IED ID | IndEnz0002004855 |
Enzyme Type ID | protease004855 |
Protein Name |
Halolysin-like extracellular serine protease Nep EC 3.4.21.- Subtilisin-like protease Nep |
Gene Name | nep |
Organism | Natrialba magadii |
Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Natrialbales Natrialbaceae Natrialba Natrialba magadii |
Enzyme Sequence | MTRDTNSNVGRRSVLKAASALGAFLGLGGVASATPGREPGPKKDEIIVGVSERVSSTEATVESKIPTNAEIVHTNETLGYVAVKFPSNAAEQARENFKRNVLQEDDIEYAEDNATYETLEVPNDPMYGQQYAPQQVNCEGAWAETYGDDDVVISVVDQGIQYDHENLAENMDGSVSDYGYDFVDDDGDPYPVSAGENHGTHVGGIAAGGTNNDTGHAGISNCSMLSARALGDGGGGSLSDIADAIQWSADQGADIINMSLGGGGFSETLDNACQYAYDEGTLLVAAAGNDHGGSVSYPAAYDSVMAVSSLDEGETLSSFSNVGPEIELAAPGGNVLSAVNWDDYDSLSGTSMASPVAAGVAGLALSAHPGLSNDELRDHLHDTAVDIGLSDDEQGYGRVDAELAVTTDPDNGDDDDDDDDDEDDPGDGECGDETNTATADGELSGGWGGNPSDTYSYELSTDNPCHATVTLDGPSSGATFDLFLTLDGRTPTTSDYDRRSYNWGADEEIEVDLDGDEELGILVDRYDGSGSYTLTIEELGS |
Enzyme Length | 541 |
Uniprot Accession Number | Q5RLZ1 |
Absorption | |
Active Site | ACT_SITE 157; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 198; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 351; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000303|PubMed:22582277" |
Activity Regulation | ACTIVITY REGULATION: Dependent on high salt concentrations for activity and stability. Strongly inhibited by the serine protease inhibitors diisopropyl fluorophosphate (DFP), phenylmethyl sulfonylfluoride (PMSF) and chymostatin. Also inhibited by denaturing agents such as SDS, urea, and HCl guanidinium. Activated by thiol-containing reducing agents such as dithiotreitol (DTT) and 2-mercaptoethanol. {ECO:0000269|PubMed:10879563}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Serine protease that hydrolyzes large proteins such as casein and gelatin. Cleaves preferentially at the carboxyl terminus of Phe, Tyr or Leu (PubMed:10879563). Is also able to catalyze peptide synthesis under different salt concentrations in the presence of dimethyl sulfoxide (DMSO) (PubMed:21039670). {ECO:0000269|PubMed:10879563, ECO:0000269|PubMed:21039670}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:10879563}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-10. {ECO:0000269|PubMed:10879563}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Compositional bias (1); Domain (1); Mutagenesis (2); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Direct protein sequencing;Hydrolase;Protease;Secreted;Serine protease;Signal;Zymogen |
Interact With | |
Induction | INDUCTION: Expressed and secreted during the transition to the stationary growth phase. Is probably up-regulated in response to factors (metabolite and/or regulatory molecule) occurring in high-density cultures. {ECO:0000269|PubMed:10879563, ECO:0000269|PubMed:20477957}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10879563, ECO:0000269|PubMed:18553052}. |
Modified Residue | |
Post Translational Modification | PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. After transport across the membrane, the propeptide is probably processed autocatalytically, yielding the mature fully active protease. {ECO:0000269|PubMed:22582277}. |
Signal Peptide | SIGNAL 1..33; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 56,454 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |