Reviewed,
UniProtKB/Swiss-Prot P81055 (PLMP_PLEOS)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peptidyl-Lys metalloendopeptidase Short name=MEP EC=3.4.24.20 Alternative name(s): PoMEP | ||
| Gene names |
| ||
| Organism | Pleurotus ostreatus (Oyster mushroom) (White-rot fungus) | ||
| Taxonomic identifier | 5322 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Pleurotaceae › Pleurotus |
Protein attributes
| Sequence length | 168 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Preferential cleavage in proteins: -Xaa-|-Lys-(in which Xaa may be Pro). |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Enzyme regulation | Inhibited by chelating agents such as EDTA and 1,10-phenanthroline. Ref.2 Ref.4 |
| Subcellular location | Secreted. Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall By similarity. |
| Sequence similarities | Belongs to the peptidase M35 family. |
| Mass spectrometry | Molecular mass is 17927 Da from positions 1 - 168. Determined by MALDI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 168 | 168 | Peptidyl-Lys metalloendopeptidase | PRO_0000078237 | |||||||
Sites | |||||||||||
| Active site | 119 | 1 | By similarity | ||||||||
| Metal binding | 118 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 122 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 131 | 1 | Zinc; catalytic By similarity | ||||||||
| Site | 134 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 6 ↔ 76 | By similarity | |||||||||
| Disulfide bond | 78 ↔ 98 | By similarity | |||||||||
Sequences
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References
| [1] | "Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies." Nonaka T., Dohmae N., Hashimoto Y., Takio K. J. Biol. Chem. 272:30032-30039(1997) [PubMed: 9374478] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY. |
| [2] | "Purification and characterization of intracellular proteinases in Pleurotus ostreatus fruiting bodies." Dohmae N., Hayashi K., Miki K., Tsumuraya Y., Hashimoto Y. Biosci. Biotechnol. Biochem. 59:2074-2080(1995) [PubMed: 8541645] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11, ENZYME REGULATION. |
| [3] | "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies." Nonaka T., Hashimoto Y., Takio K. J. Biochem. 124:157-162(1998) [PubMed: 9644258] [Abstract] Cited for: SUBSTRATE SPECIFICITY. |
| [4] | "Purification and partial characterization of a fibrinolytic protease in Pleurotus ostreatus." Choi H.-S., Shin H.-H. Mycologia 90:674-679(1998) [Agricola: IND21804865] Cited for: ENZYME REGULATION, ZINC-BINDING. |
Cross-references
3D structure databases | |
|---|---|
| HSSP | HSSP built from PDB template 1G12 based on UniProtKB P81054. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.20. 16687. |
Family and domain databases | |
| InterPro | IPR006025. Pept_M_Zn_BS. [Graphical view] |
| PROSITE | PS00142. ZINC_PROTEASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLMP_PLEOS | ||||||||
| Accession | Primary (citable) accession number: P81055 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


