Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P81054 (PLMP_GRIFR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-Lys metalloendopeptidase

Short name=MEP
EC=3.4.24.20
Alternative name(s):
GfMEP
Gene names
Name:MEP
OrganismGrifola frondosa (Maitake) (Polyporus frondosus)
Taxonomic identifier5627 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeGrifola

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Enzyme regulation

Inhibited by chelating agents such as EDTA and 1,10-phenanthroline. Ref.3

Subcellular location

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

Sequence similarities

Belongs to the peptidase M35 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to pH 10. Ref.3

Temperature dependence:

Thermostable for 3 hours up to 80 degrees Celsius.

Mass spectrometry

Molecular mass is 18028 Da from positions 182 - 348. Determined by MALDI. Ref.2

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Propeptide19 – 181163
PRO_0000043399
Chain182 – 348167Peptidyl-Lys metalloendopeptidase
PRO_0000043400

Regions

Compositional bias193 – 2019Poly-Ala

Sites

Active site2991 By similarity
Metal binding2981Zinc; catalytic
Metal binding3021Zinc; catalytic
Metal binding3111Zinc; catalytic
Site3141Transition state stabilizer Probable

Amino acid modifications

Glycosylation2231O-linked (Man); partial
Disulfide bond186 ↔ 256
Disulfide bond258 ↔ 278

Secondary structure

............................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81054 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 5F3859F10B423C79

FASTA34836,879
        10         20         30         40         50         60 
MFSSVMVALV SLAVAVSANP GLSLKVSGPE AVDGVNNLKV VTTITNTGDE TLKLLNDPRG 

        70         80         90        100        110        120 
ALHTMPTDTF AITNESGETP SFIGVKVKYV PSMAAKSTGE NVFAVIAPGQ SVNVEHDLSA 

       130        140        150        160        170        180 
AYNFTSSGAG TYALEALNVF NYIDPETNEP VEIWADAEAH TTAVSGKLAV VRATPTLTRP 

       190        200        210        220        230        240 
VTYNGCSSSE QSALAAAASA AQSYVAESLS YLQTHTAATP RYTTWFGSYI SSRHSTVLQH 

       250        260        270        280        290        300 
YTDMNSNDFS SYSFDCTCTA AGTFAYVYPN RFGTVYLCGA FWKAPTTGTD SQAGTLVHES 

       310        320        330        340 
SHFTRNGGTK DYAYGQAAAK SLATMDPDKA VMNADNHEYF SENNPAQS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB076805 mRNA. Translation: BAB82381.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G12X-ray1.60A182-348[»]
1GE5X-ray2.00A182-348[»]
1GE6X-ray2.20A182-348[»]
1GE7X-ray2.00A/B182-348[»]
ProteinModelPortalP81054.
SMRP81054. Positions 182-348.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM35.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.24.20. 2512.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR029463. Lys_MEP.
IPR024079. MetalloPept_cat_dom.
[Graphical view]
PfamPF14521. Aspzincin_M35. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81054.

Entry information

Entry namePLMP_GRIFR
AccessionPrimary (citable) accession number: P81054
Secondary accession number(s): Q8WZH2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references