Reviewed, UniProtKB/Swiss-Prot P81054 (PLMP_GRIFR)

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)

Taxonomic identifier

5627 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › 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. 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: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding 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

18

Ref.1

Propeptide

19 – 181

163

Ref.3 Ref.2

PRO_0000043399

Chain

182 – 348

167

Peptidyl-Lys metalloendopeptidase

PRO_0000043400

Regions

Compositional bias

193 – 201

9

Poly-Ala

Sites

Active site

299

1

By similarity

Metal binding

298

1

Zinc; catalytic

Metal binding

302

1

Zinc; catalytic

Metal binding

311

1

Zinc; catalytic

Site

314

1

Transition state stabilizer Probable

Amino acid modifications

Glycosylation

223

1

O-linked (Man); partial

Disulfide bond

186 ↔ 256

Disulfide bond

258 ↔ 278

Secondary structure

1

.

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.

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348

Helix Strand Turn

Details...

Beta strand

183 – 185

3

Helix

188 – 214

27

Helix

220 – 226

7

Helix

231 – 245

15

Helix

249 – 251

3

Beta strand

253 – 255

3

Beta strand

274 – 277

4

Helix

279 – 283

5

Beta strand

286 – 288

3

Helix

292 – 302

11

Helix

304 – 306

3

Helix

315 – 325

11

Helix

327 – 330

4

Helix

334 – 342

9

Sequences

	Sequence		Length	Mass (Da)
	P81054-1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 5F3859F10B423C79	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

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: 12501439] [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: 9374478] [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: 8749321] [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: 9644258] [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: 11223512] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MATURE FORM.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB076805 mRNA. Translation: BAB82381.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M35.004.

Enzyme and pathway databases

BRENDA

3.4.24.20. 19001.

Family and domain databases

InterPro

IPR006025. Pept_M_Zn_BS.
IPR001384. Peptidase_M35.
[Graphical view]

Pfam

PF02102. Peptidase_M35. 1 hit.
[Graphical view]

PROSITE

PS00142. ZINC_PROTEASE. False negative.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)