PLMP_GRIFR
ID PLMP_GRIFR Reviewed; 348 AA.
AC P81054; Q8WZH2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Peptidyl-Lys metalloendopeptidase;
DE Short=MEP;
DE EC=3.4.24.20;
DE AltName: Full=GfMEP;
DE Flags: Precursor;
GN Name=MEP;
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-28; 96-105 AND
RP 167-178.
RC STRAIN=S.F. Gray;
RX PubMed=12501439; DOI=10.2323/jgam.48.287;
RA Saito T., Dohmae N., Tsujimoto M., Takio K.;
RT "PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys
RT metalloendopeptidase precursor of Grifola frondosa.";
RL J. Gen. Appl. Microbiol. 48:287-292(2002).
RN [2]
RP PROTEIN SEQUENCE OF 182-348, GLYCOSYLATION AT THR-223, AND MASS
RP SPECTROMETRY.
RX 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-lysine
RT bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies.";
RL J. Biol. Chem. 272:30032-30039(1997).
RN [3]
RP PROTEIN SEQUENCE OF 182-196, BIOPHYSICOCHEMICAL PROPERTIES, ZINC-BINDING,
RP ACTIVITY REGULATION, AND BINDING TO BETA-GLUCANS AND CHITIN.
RX PubMed=8749321; DOI=10.1093/jb/118.5.1014;
RA Nonaka T., Ishikawa H., Tsumuraya Y., Hashimoto Y., Dohmae N., Takio K.;
RT "Characterization of a thermostable lysine-specific metalloendopeptidase
RT from the fruiting bodies of a basidiomycete, Grifola frondosa.";
RL J. Biochem. 118:1014-1020(1995).
RN [4]
RP SUBSTRATE SPECIFICITY.
RX PubMed=9644258; DOI=10.1093/oxfordjournals.jbchem.a022074;
RA Nonaka T., Hashimoto Y., Takio K.;
RT "Kinetic characterization of lysine-specific metalloendopeptidases from
RT Grifola frondosa and Pleurotus ostreatus fruiting bodies.";
RL J. Biochem. 124:157-162(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MATURE FORM IN COMPLEX WITH ZINC,
RP COFACTOR, ACTIVE SITE, AND DISULFIDE BONDS.
RX PubMed=11223512; DOI=10.1107/s0907444900019740;
RA Hori T., Kumasaka T., Yamamoto M., Nonaka N., Tanaka N., Hashimoto Y.,
RA Ueki U., Takio K.;
RT "Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa:
RT implications for the catalytic mechanism and substrate specificity based on
RT several different crystal forms.";
RL Acta Crystallogr. D 57:361-368(2001).
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:11223512};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11223512};
CC -!- ACTIVITY REGULATION: Inhibited by chelating agents such as EDTA and
CC 1,10-phenanthroline. {ECO:0000269|PubMed:8749321}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to
CC pH 10. {ECO:0000269|PubMed:8749321};
CC Temperature dependence:
CC Thermostable for 3 hours up to 80 degrees Celsius.
CC {ECO:0000269|PubMed:8749321};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Binds strongly to
CC beta-1,3-glucan and chitin, major polysaccharides constituting the
CC fungal cell wall.
CC -!- MASS SPECTROMETRY: Mass=18028; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9374478};
CC -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR EMBL; AB076805; BAB82381.1; -; mRNA.
DR PDB; 1G12; X-ray; 1.60 A; A=182-348.
DR PDB; 1GE5; X-ray; 2.00 A; A=182-348.
DR PDB; 1GE6; X-ray; 2.20 A; A=182-348.
DR PDB; 1GE7; X-ray; 2.00 A; A/B=182-348.
DR PDBsum; 1G12; -.
DR PDBsum; 1GE5; -.
DR PDBsum; 1GE6; -.
DR PDBsum; 1GE7; -.
DR AlphaFoldDB; P81054; -.
DR SMR; P81054; -.
DR MEROPS; M35.004; -.
DR iPTMnet; P81054; -.
DR KEGG; ag:BAB82381; -.
DR BRENDA; 3.4.24.20; 2512.
DR EvolutionaryTrace; P81054; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:12501439"
FT PROPEP 19..181
FT /evidence="ECO:0000269|PubMed:8749321,
FT ECO:0000269|PubMed:9374478"
FT /id="PRO_0000043399"
FT CHAIN 182..348
FT /note="Peptidyl-Lys metalloendopeptidase"
FT /id="PRO_0000043400"
FT ACT_SITE 299
FT /evidence="ECO:0000269|PubMed:11223512"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11223512"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11223512"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11223512"
FT SITE 314
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT CARBOHYD 223
FT /note="O-linked (Man) threonine; partial"
FT /evidence="ECO:0000269|PubMed:9374478"
FT DISULFID 186..256
FT /evidence="ECO:0000269|PubMed:11223512"
FT DISULFID 258..278
FT /evidence="ECO:0000269|PubMed:11223512"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 188..214
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1G12"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1G12"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:1G12"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1G12"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:1G12"
SQ SEQUENCE 348 AA; 36879 MW; 5F3859F10B423C79 CRC64;
MFSSVMVALV SLAVAVSANP GLSLKVSGPE AVDGVNNLKV VTTITNTGDE TLKLLNDPRG
ALHTMPTDTF AITNESGETP SFIGVKVKYV PSMAAKSTGE NVFAVIAPGQ SVNVEHDLSA
AYNFTSSGAG TYALEALNVF NYIDPETNEP VEIWADAEAH TTAVSGKLAV VRATPTLTRP
VTYNGCSSSE QSALAAAASA AQSYVAESLS YLQTHTAATP RYTTWFGSYI SSRHSTVLQH
YTDMNSNDFS SYSFDCTCTA AGTFAYVYPN RFGTVYLCGA FWKAPTTGTD SQAGTLVHES
SHFTRNGGTK DYAYGQAAAK SLATMDPDKA VMNADNHEYF SENNPAQS
