ID   PLMP_PLEOS     STANDARD;      PRT;   168 AA.
AC   P81055;
DT   15-JUL-1998 (Rel. 36, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20) (MEP) (POMEP).
OS   Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=5322;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   MEDLINE=98043693; PubMed=9374478; DOI=10.1074/jbc.272.48.30032;
RA   Nonaka T., Dohmae N., Hashimoto Y., Takio K.;
RT   "Amino acid sequences of metalloendopeptidases specific for acyl-
RT   lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting
RT   bodies.";
RL   J. Biol. Chem. 272:30032-30039(1997).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage in proteins: Xaa-|-Lys
CC       (in which Xaa may be Pro).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: MW=17927; METHOD=MALDI; RANGE=1-168;
CC       NOTE=Ref.1.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family.
DR   HSSP; P81054; 1G12.
DR   MEROPS; M35.004; -.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG.
KW   Direct protein sequencing; Hydrolase; Metalloprotease; Zinc.
FT   DISULFID      6     76       By similarity.
FT   DISULFID     78     98       By similarity.
FT   METAL       118    118       Zinc (catalytic) (By similarity).
FT   ACT_SITE    119    119       By similarity.
FT   METAL       122    122       Zinc (catalytic) (By similarity).
SQ   SEQUENCE   168 AA;  17925 MW;  78E5556CB1566547 CRC64;
     ATFVGCSATR QTQLNAAASQ AQTYAANALS YLNSHTSSTT RYTTWFGTFV TSRYNTVLSH
     FSSISSNTFS SYTFDCTCSD SGTYAFVNPS NFGYVTLCGA FWNAPVAGTD SRGGTLIHES
     SHFTRNGGTD DHVYGQAGAQ SLARSNPAQA IDNADSHEYF AENNPALA
//