ID   PLMP_ARMME              Reviewed;         351 AA.
AC   Q9Y7F7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Peptidyl-Lys metalloendopeptidase;
DE            Short=MEP;
DE            EC=3.4.24.20;
DE   AltName: Full=AmMEP;
DE   Flags: Precursor;
GN   Name=MEP;
OS   Armillaria mellea (Shoestring root rot fungus) (Honey mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47429;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Vad K., Thim L.;
RT   "Cloning and expression of an Armillaria mellea metalloendopeptidase.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 184-209.
RX   PubMed=10448068; DOI=10.1006/bbrc.1999.1151;
RA   Healy V., O'Connell J., McCarthy T.V., Doonan S.;
RT   "The lysine-specific proteinase from Armillaria mellea is a member of a
RT   novel class of metalloendopeptidases located in Basidiomycetes.";
RL   Biochem. Biophys. Res. Commun. 262:60-63(1999).
RN   [3]
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   ZINC-BINDING, AND COFACTOR.
RX   PubMed=23849; DOI=10.1016/0005-2744(78)90087-6;
RA   Lewis W.G., Basford J.M., Walton P.L.;
RT   "Specificity and inhibition studies of Armillaria mellea protease.";
RL   Biochim. Biophys. Acta 522:551-560(1978).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa
CC         may be Pro).; EC=3.4.24.20;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:23849};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23849};
CC   -!- ACTIVITY REGULATION: Inhibited by chelating agents such as imidazole,
CC       alpha,alpha'-bipyridine, and 1,10-phenanthroline.
CC       {ECO:0000269|PubMed:23849}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-7.5. Active from pH 5.25 to pH 9.
CC         {ECO:0000269|PubMed:23849};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Binds strongly to
CC       beta-1,3-glucan and chitin, major polysaccharides constituting the
CC       fungal cell wall. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; AJ238718; CAB42792.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7F7; -.
DR   SMR; Q9Y7F7; -.
DR   MEROPS; M35.004; -.
DR   KEGG; ag:CAB42792; -.
DR   BRENDA; 3.4.24.20; 426.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd11306; M35_peptidyl-Lys; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029463; Lys_MEP.
DR   InterPro; IPR034115; M35_peptidyl-Lys.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   Pfam; PF14521; Aspzincin_M35; 1.
DR   SMART; SM01351; Aspzincin_M35; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..183
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000043401"
FT   CHAIN           184..351
FT                   /note="Peptidyl-Lys metalloendopeptidase"
FT                   /id="PRO_0000043402"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   SITE            317
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..259
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   DISULFID        261..281
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   CONFLICT        189
FT                   /note="C -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="A -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  37551 MW;  396F2999FFD06833 CRC64;
     MFSLSSRFFL YSLCLSAVAV SAAPGLSLSL SGADSVVDVE NLNVAATLTN TGDTTLKILN
     DPSSILSSKF ATHTFDISSD NGSPAFTGVK VKYDPNYVVK KNADSSFTVL APGESVTVNH
     ALGAAYNFTG SGAASYSIEP SSLFYYVDPD TNELASINAD TQQHTTKISG TLAVARRSNL
     GKRISYNGCT SSRQTTLVSA AAAAQTYAQS SYNYLSSHTA STTRYVTWFG PYTSARHSTV
     LSCFSNMLAY PYANYEYDCT CTESDVYAYV YPSQFGTIYL CGAFWQTTTT GTDSRGGTLI
     HESSHFTIIC GTQDYAYGQS AAKSLASSNP SEAIKNADNY EYFAENNPAQ S