Detail Information for IndEnz0002004855
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