ID   SNPA_STRCH              Reviewed;         215 AA.
AC   P43164;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Extracellular small neutral protease;
DE            EC=3.4.24.77;
DE   AltName: Full=Extracellular metalloprotease;
DE   AltName: Full=Snapalysin;
DE   Flags: Precursor;
GN   Name=snpA; Synonyms=mprA;
OS   Streptomyces coelicolor.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=1902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 3030 / Mueller;
RX   PubMed=1406267; DOI=10.1111/j.1365-2958.1992.tb01402.x;
RA   Dammann T., Wohlleben W.;
RT   "A metalloprotease gene from Streptomyces coelicolor 'Muller' and its
RT   transcriptional activator, a member of the LysR family.";
RL   Mol. Microbiol. 6:2267-2278(1992).
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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M7 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z11929; CAA77985.1; -; Genomic_DNA.
DR   PIR; S25187; S25187.
DR   AlphaFoldDB; P43164; -.
DR   SMR; P43164; -.
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   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028644"
FT   CHAIN           ?..215
FT                   /note="Extracellular small neutral protease"
FT                   /id="PRO_0000028645"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   DISULFID        173..186
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
SQ   SEQUENCE   215 AA;  22208 MW;  A1E5260D7787C2ED CRC64;
     MRMTRAASAL AGLGLAVAAA LGSVAPASAA AETSTPRSVA AYEASTENAA ATRAFQEAVM
     KAVAEKRAAN PGALAVTVTY DASAAPTFRS QIASSTSIWN GAVSNVRLQE GSNADFTYRE
     GNDPRGSYAS TEAHGRGYIF LDYAQNQQYN STRVTTHETG HVLGLPDTYS GPCSQLMSGG
     GPGPSCTNAQ PDSAERSRVE QLWANGLAEA AAEVR