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P81054

- PLMP_GRIFR

UniProt

P81054 - PLMP_GRIFR

Protein

Peptidyl-Lys metalloendopeptidase

Gene

MEP

Organism
Grifola frondosa (Maitake) (Polyporus frondosus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage in proteins: -Xaa-|-Lys-(in which Xaa may be Pro).

    Cofactori

    Binds 1 zinc ion per subunit.

    Enzyme regulationi

    Inhibited by chelating agents such as EDTA and 1,10-phenanthroline.1 Publication

    pH dependencei

    Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to pH 10.1 Publication

    Temperature dependencei

    Thermostable for 3 hours up to 80 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi298 – 2981Zinc; catalytic
    Active sitei299 – 2991By similarity
    Metal bindingi302 – 3021Zinc; catalytic
    Metal bindingi311 – 3111Zinc; catalytic
    Sitei314 – 3141Transition state stabilizerCurated

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.20. 2512.

    Protein family/group databases

    MEROPSiM35.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-Lys metalloendopeptidase (EC:3.4.24.20)
    Short name:
    MEP
    Alternative name(s):
    GfMEP
    Gene namesi
    Name:MEP
    OrganismiGrifola frondosa (Maitake) (Polyporus frondosus)
    Taxonomic identifieri5627 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeGrifola

    Subcellular locationi

    Secreted Curated
    Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Propeptidei19 – 1811632 PublicationsPRO_0000043399Add
    BLAST
    Chaini182 – 348167Peptidyl-Lys metalloendopeptidasePRO_0000043400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi186 ↔ 256
    Glycosylationi223 – 2231O-linked (Man); partial
    Disulfide bondi258 ↔ 278

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi183 – 1853
    Helixi188 – 21427
    Helixi220 – 2267
    Helixi231 – 24515
    Helixi249 – 2513
    Beta strandi253 – 2553
    Beta strandi274 – 2774
    Helixi279 – 2835
    Beta strandi286 – 2883
    Helixi292 – 30211
    Helixi304 – 3063
    Helixi315 – 32511
    Helixi327 – 3304
    Helixi334 – 3429

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G12X-ray1.60A182-348[»]
    1GE5X-ray2.00A182-348[»]
    1GE6X-ray2.20A182-348[»]
    1GE7X-ray2.00A/B182-348[»]
    ProteinModelPortaliP81054.
    SMRiP81054. Positions 182-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81054.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi193 – 2019Poly-Ala

    Sequence similaritiesi

    Belongs to the peptidase M35 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR029463. Lys_MEP.
    IPR024079. MetalloPept_cat_dom.
    [Graphical view]
    PfamiPF14521. Aspzincin_M35. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P81054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSSVMVALV SLAVAVSANP GLSLKVSGPE AVDGVNNLKV VTTITNTGDE    50
    TLKLLNDPRG ALHTMPTDTF AITNESGETP SFIGVKVKYV PSMAAKSTGE 100
    NVFAVIAPGQ SVNVEHDLSA AYNFTSSGAG TYALEALNVF NYIDPETNEP 150
    VEIWADAEAH TTAVSGKLAV VRATPTLTRP VTYNGCSSSE QSALAAAASA 200
    AQSYVAESLS YLQTHTAATP RYTTWFGSYI SSRHSTVLQH YTDMNSNDFS 250
    SYSFDCTCTA AGTFAYVYPN RFGTVYLCGA FWKAPTTGTD SQAGTLVHES 300
    SHFTRNGGTK DYAYGQAAAK SLATMDPDKA VMNADNHEYF SENNPAQS 348
    Length:348
    Mass (Da):36,879
    Last modified:December 6, 2005 - v2
    Checksum:i5F3859F10B423C79
    GO

    Mass spectrometryi

    Molecular mass is 18028 Da from positions 182 - 348. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB076805 mRNA. Translation: BAB82381.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB076805 mRNA. Translation: BAB82381.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G12 X-ray 1.60 A 182-348 [» ]
    1GE5 X-ray 2.00 A 182-348 [» ]
    1GE6 X-ray 2.20 A 182-348 [» ]
    1GE7 X-ray 2.00 A/B 182-348 [» ]
    ProteinModelPortali P81054.
    SMRi P81054. Positions 182-348.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M35.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.24.20. 2512.

    Miscellaneous databases

    EvolutionaryTracei P81054.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR029463. Lys_MEP.
    IPR024079. MetalloPept_cat_dom.
    [Graphical view ]
    Pfami PF14521. Aspzincin_M35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa."
      Saito T., Dohmae N., Tsujimoto M., Takio K.
      J. Gen. Appl. Microbiol. 48:287-292(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-28; 96-105 AND 167-178.
      Strain: S.F. Gray.
    2. "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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-348, MASS SPECTROMETRY.
    3. "Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa."
      Nonaka T., Ishikawa H., Tsumuraya Y., Hashimoto Y., Dohmae N., Takio K.
      J. Biochem. 118:1014-1020(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-196, BIOPHYSICOCHEMICAL PROPERTIES, ZINC-BINDING, ENZYME REGULATION, BINDING TO BETA-GLUCANS AND CHITIN.
    4. "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] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    5. "Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms."
      Hori T., Kumasaka T., Yamamoto M., Nonaka N., Tanaka N., Hashimoto Y., Ueki U., Takio K.
      Acta Crystallogr. D 57:361-368(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MATURE FORM.

    Entry informationi

    Entry nameiPLMP_GRIFR
    AccessioniPrimary (citable) accession number: P81054
    Secondary accession number(s): Q8WZH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3