ID   SNPA_STRCS              Reviewed;         132 AA.
AC   P56406;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Extracellular small neutral protease;
DE            EC=3.4.24.77;
DE   AltName: Full=SCNP;
DE   AltName: Full=Snapalysin;
GN   Name=snpA;
OS   Streptomyces caespitosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=53502;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7588817; DOI=10.1111/j.1432-1033.1995.683_2.x;
RA   Harada S., Kinoshita T., Kasai N., Tsunasawa S., Sakiyama F.;
RT   "Complete amino acid sequence of a zinc metalloendoprotease from
RT   Streptomyces caespitosus.";
RL   Eur. J. Biochem. 233:683-686(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC,
RP   COFACTOR, AND DISULFIDE BONDS.
RX   PubMed=9089404; DOI=10.1093/oxfordjournals.jbchem.a021587;
RA   Kurisu G., Kinoshita T., Sugimoto A., Nagara A., Kai Y., Kasai N.,
RA   Harada S.;
RT   "Structure of the zinc endoprotease from Streptomyces caespitosus.";
RL   J. Biochem. 121:304-308(1997).
CC   -!- FUNCTION: Specifically hydrolyzes the peptide bond at the imino side of
CC       aromatic residues.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes proteins with a preference for Tyr or Phe in the
CC         P1' position. Has no action on amino-acid p-nitroanilides.;
CC         EC=3.4.24.77;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000305|PubMed:9089404};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:9089404};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:9089404};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9089404};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M7 family. {ECO:0000305}.
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DR   PIR; S63978; S63978.
DR   PDB; 1C7K; X-ray; 1.00 A; A=1-132.
DR   PDB; 1KUH; X-ray; 1.60 A; A=1-132.
DR   PDB; 4HX3; X-ray; 2.70 A; A/C/E/G/I/K=2-132.
DR   PDBsum; 1C7K; -.
DR   PDBsum; 1KUH; -.
DR   PDBsum; 4HX3; -.
DR   AlphaFoldDB; P56406; -.
DR   SMR; P56406; -.
DR   MEROPS; M07.001; -.
DR   EvolutionaryTrace; P56406; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000013; Peptidase_M7.
DR   Pfam; PF02031; Peptidase_M7; 1.
DR   PIRSF; PIRSF016573; Peptidase_M7; 1.
DR   PRINTS; PR00787; NEUTRALPTASE.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           1..132
FT                   /note="Extracellular small neutral protease"
FT                   /id="PRO_0000078176"
FT   ACT_SITE        84
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:9089404"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:9089404"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:9089404"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:9089404"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:9089404"
FT   DISULFID        99..112
FT                   /evidence="ECO:0000269|PubMed:7588817,
FT                   ECO:0000269|PubMed:9089404"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           69..74
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           77..89
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   TURN            105..108
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:1C7K"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:1C7K"
SQ   SEQUENCE   132 AA;  14376 MW;  7CB988AFC2F0B1E4 CRC64;
     TVTVTYDPSN APSFQQEIAN AAQIWNSSVR NVQLRAGGNA DFSYYEGNDS RGSYAQTDGH
     GRGYIFLDYQ QNQQYDSTRV TAHETGHVLG LPDHYQGPCS ELMSGGGPGP SCTNPYPNAQ
     ERSRVNALWA NG