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Reviewed, UniProtKB/Swiss-Prot P81055 (PLMP_PLEOS)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-Lys metalloendopeptidase
      Short name=MEP
    EC=3.4.24.20
Alternative name(s):
    PoMEP
Gene names
Name: MEP
OrganismPleurotus ostreatus (Oyster mushroom) (White-rot fungus)
Taxonomic identifier5322 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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 componentSecreted
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Peptidyl-Lys metalloendopeptidase
PRO_0000078237

Sites

Active site1191 By similarity
Metal binding1181Zinc; catalytic By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1311Zinc; catalytic By similarity
Site1341Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond6 ↔ 76 By similarity
Disulfide bond78 ↔ 98 By similarity

Sequences

Sequence LengthMass (Da)Tools
P81055-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 78E5556CB1566547

FASTA16817,925
        10         20         30         40         50         60 
ATFVGCSATR QTQLNAAASQ AQTYAANALS YLNSHTSSTT RYTTWFGTFV TSRYNTVLSH 

        70         80         90        100        110        120 
FSSISSNTFS SYTFDCTCSD SGTYAFVNPS NFGYVTLCGA FWNAPVAGTD SRGGTLIHES 

       130        140        150        160 
SHFTRNGGTD DHVYGQAGAQ SLARSNPAQA IDNADSHEYF AENNPALA 

« Hide

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

HSSPHSSP built from PDB template 1G12 based on UniProtKB P81054.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.4.24.20. 16687.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMP_PLEOS
AccessionPrimary (citable) accession number: P81055
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents