ID   SNPA_STRS5              Reviewed;         229 AA.
AC   P43163;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Extracellular small neutral protease;
DE            EC=3.4.24.77;
DE   AltName: Full=Snapalysin;
DE   Flags: Precursor;
GN   Name=snpA;
OS   Streptomyces sp. (strain C5).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=45212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 82-101.
RX   PubMed=1569011; DOI=10.1128/jb.174.9.2797-2808.1992;
RA   Lampel J.S., Aphale J.S., Lampel K.A., Strohl W.R.;
RT   "Cloning and sequencing of a gene encoding a novel extracellular neutral
RT   proteinase from Streptomyces sp. strain C5 and expression of the gene in
RT   Streptomyces lividans 1326.";
RL   J. Bacteriol. 174:2797-2808(1992).
CC   -!- FUNCTION: Milk hydrolyzing.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M7 family. {ECO:0000305}.
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DR   EMBL; M86606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P43163; -.
DR   SMR; P43163; -.
DR   MEROPS; M07.001; -.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..81
FT                   /evidence="ECO:0000269|PubMed:1569011"
FT                   /id="PRO_0000028650"
FT   CHAIN           82..229
FT                   /note="Extracellular small neutral protease"
FT                   /id="PRO_0000028651"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   DISULFID        182..195
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
SQ   SEQUENCE   229 AA;  23607 MW;  60B1CA358C297749 CRC64;
     MRMPLSVLTA AGLSLATLGL GTAGPASATP TAEGAPVVAY DGSPSAGSPA DAKAEAAANR
     AFFEAVLRSV AEKRAANPKS TAAVTVVYNA SGAPSFATQI ARGTQIWNSS VSNVRLQAGS
     SGVDFTYREG NDPRGSYAST DGHGRGYIFL DYRQNQTYDS TRVTAHETGH VLGLPDHYSG
     PCSELMSGGG PGPSCTNAYP NSAERSRVNQ LWANGFAAAM DKALEKSAR