Peptidyl-Lys metalloendopeptidase precursor - Grifola frondosa (Maitake)

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P81054 (PLMP_GRIFR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peptidyl-Lys metalloendopeptidase
Short name=MEP
EC=3.4.24.20

Alternative name(s):
GfMEP

Gene names

Name:

MEP

Organism

Grifola frondosa (Maitake) (Polyporus frondosus)

Taxonomic identifier

5627 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Schizophyllaceae › Grifola

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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 component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Ref.1

Propeptide

19 – 181

163

PRO_0000043399

Chain

182 – 348

167

Peptidyl-Lys metalloendopeptidase

PRO_0000043400

Regions

Compositional bias

193 – 201

Poly-Ala

Sites

Active site

299

By similarity

Metal binding

298

Zinc; catalytic

Metal binding

302

Zinc; catalytic

Metal binding

311

Zinc; catalytic

Site

314

Transition state stabilizer Probable

Amino acid modifications

Glycosylation

223

O-linked (Man); partial

Disulfide bond

186 ↔ 256

Disulfide bond

258 ↔ 278

Secondary structure

348

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P81054 [UniParc].

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

FASTA

348

36,879

        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

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	[»]

ProteinModelPortal

P81054.

SMR

P81054. Positions 182-348.

ModBase

Search...

Protein family/group databases

MEROPS

M35.004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.24.20. 2512.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.

InterPro

IPR024079. MetalloPept_cat_dom.
[Graphical view]

PROSITE

PS00142. ZINC_PROTEASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P81054.

Entry information

Entry name

PLMP_GRIFR

Accession

Primary (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:	April 3, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents