ID   MYCO_STRCI              Reviewed;         550 AA.
AC   P20910;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Mycolysin;
DE            EC=3.4.24.31;
DE   AltName: Full=Neutral metalloproteinase;
DE            Short=NPR;
DE   AltName: Full=Pronase;
DE   Flags: Precursor;
GN   Name=npr;
OS   Streptomyces cacaoi.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YM15;
RX   PubMed=2341042; DOI=10.1016/0378-1119(90)90063-w;
RA   Chang P.-C., Kuo T.-C., Tsugita A., Lee Y.-H.W.;
RT   "Extracellular metalloprotease gene of Streptomyces cacaoi: structure,
RT   nucleotide sequence and characterization of the cloned gene product.";
RL   Gene 88:87-95(1990).
RN   [2]
RP   PROTEOLYTIC PROCESSING, ACTIVE SITE, ZINC-LIGANDS, AND MUTAGENESIS.
RX   PubMed=1740443; DOI=10.1016/s0021-9258(19)50618-4;
RA   Chang P.-C., Lee Y.-H.W.;
RT   "Extracellular autoprocessing of a metalloprotease from Streptomyces
RT   cacaoi.";
RL   J. Biol. Chem. 267:3952-3958(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'.; EC=3.4.24.31;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M5 family. {ECO:0000305}.
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DR   EMBL; M37055; AAA26789.1; -; Genomic_DNA.
DR   PIR; JQ0530; HYSMCA.
DR   AlphaFoldDB; P20910; -.
DR   MEROPS; M05.001; -.
DR   KEGG; ag:AAA26789; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL          1..34
FT   PROPEP          35..205
FT                   /id="PRO_0000028640"
FT   CHAIN           206..550
FT                   /note="Mycolysin"
FT                   /id="PRO_0000028641"
FT   REGION          160..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000269|PubMed:1740443"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:1740443"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:1740443"
FT   BINDING         445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:1740443"
SQ   SEQUENCE   550 AA;  58678 MW;  C9FF9C998044D8BE CRC64;
     MPMFRIRLPK PAALIAAGGI GACIATVAVP SAYAAAPAPA DSRLGVTASL DRLPSIGERS
     TLTVNITAET DVKRAGLSLQ LPPALRIVDR NPSLAAPTTD PFGQRTSRTL TLTPGTRTIE
     LEVKAVATGP AQIQADISDI DRPDPRRAGH ASVELTIGKA KGSTAKGMSV TKADATPVSG
     PTTPGRPVRP GAAAPAAPST PPQAAAPGKR YAPVCVSGTL RNRFQSSEGG SWNSKASRDL
     PVSNANVTLW GRATAGGGTQ KLAAGLTGNG DGTFKLCYTP STSVTSQVWA EFQTQAGTMW
     SVVDGYNRRY STTSNALSNV SGNKSLGTVY ANSGQSRAWH AFDTLNKLWW DRGSTSTCWT
     SNQRDGRCTP ITVQWYPGST DGTYWTNRDD KVHLADSDPD SGHTTVHEAG HSLMGKLYNG
     WWPYVTNCSP HYINRTSSTT CGWTEGFADA VAFHTFKDTV MTWGNGSSMN LANDRGTRGM
     DWGDACEARV GTALVDLWSQ VDGGWTKSNT MMSRERQSTF REYFLTDRPA YGLDSGPKAR
     NILYGHTIQY