P81054 · PLMP_GRIFR
- ProteinPeptidyl-Lys metalloendopeptidase
- GeneMEP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids348 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited by chelating agents such as EDTA and 1,10-phenanthroline.
pH Dependence
Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to pH 10.
Temperature Dependence
Thermostable for 3 hours up to 80 degrees Celsius.
Features
Showing features for binding site, active site, site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-Lys metalloendopeptidase
- EC number
- Short namesMEP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Grifolaceae > Grifola
Accessions
- Primary accessionP81054
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MFSSVMVALVSLAVAVSA | ||||||
Propeptide | PRO_0000043399 | 19-181 | ||||
Sequence: NPGLSLKVSGPEAVDGVNNLKVVTTITNTGDETLKLLNDPRGALHTMPTDTFAITNESGETPSFIGVKVKYVPSMAAKSTGENVFAVIAPGQSVNVEHDLSAAYNFTSSGAGTYALEALNVFNYIDPETNEPVEIWADAEAHTTAVSGKLAVVRATPTLTRPV | ||||||
Chain | PRO_0000043400 | 182-348 | Peptidyl-Lys metalloendopeptidase | |||
Sequence: TYNGCSSSEQSALAAAASAAQSYVAESLSYLQTHTAATPRYTTWFGSYISSRHSTVLQHYTDMNSNDFSSYSFDCTCTAAGTFAYVYPNRFGTVYLCGAFWKAPTTGTDSQAGTLVHESSHFTRNGGTKDYAYGQAAAKSLATMDPDKAVMNADNHEYFSENNPAQS | ||||||
Disulfide bond | 186↔256 | |||||
Sequence: CSSSEQSALAAAASAAQSYVAESLSYLQTHTAATPRYTTWFGSYISSRHSTVLQHYTDMNSNDFSSYSFDC | ||||||
Glycosylation | 223 | O-linked (Man) threonine; partial | ||||
Sequence: T | ||||||
Disulfide bond | 258↔278 | |||||
Sequence: CTAAGTFAYVYPNRFGTVYLC |
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length348
- Mass (Da)36,879
- Last updated2005-12-06 v2
- Checksum5F3859F10B423C79
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB076805 EMBL· GenBank· DDBJ | BAB82381.1 EMBL· GenBank· DDBJ | mRNA |