ID   SNPA_STRCO              Reviewed;         227 AA.
AC   P0A3Z7; P43162;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=lmp, mprA, mprA2, prt; OrderedLocusNames=SCO7432;
GN   ORFNames=SC6D11.28c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M7 family. {ECO:0000305}.
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DR   EMBL; AL939131; CAB76351.1; -; Genomic_DNA.
DR   RefSeq; NP_631481.1; NC_003888.3.
DR   RefSeq; WP_003971712.1; NZ_VNID01000005.1.
DR   AlphaFoldDB; P0A3Z7; -.
DR   SMR; P0A3Z7; -.
DR   STRING; 100226.SCO7432; -.
DR   MEROPS; M07.001; -.
DR   GeneID; 1102870; -.
DR   KEGG; sco:SCO7432; -.
DR   PATRIC; fig|100226.15.peg.7542; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_087297_0_0_11; -.
DR   OMA; RSTQIWN; -.
DR   Proteomes; UP000001973; Chromosome.
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   Calcium; Disulfide bond; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..42
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028646"
FT   CHAIN           43..227
FT                   /note="Extracellular small neutral protease"
FT                   /id="PRO_0000028647"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   BINDING         163
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   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
FT   DISULFID        179..192
FT                   /evidence="ECO:0000250|UniProtKB:P56406"
SQ   SEQUENCE   227 AA;  23765 MW;  7CAE68EADD8678CF CRC64;
     MRITLPLLST AVGLGLTAAV LGTGPAATAA APQEPVRAAQ LGYQPSAGSG EDAAANRAFF
     EAVVKSVAEK RAANPSAAAA VTVYYSATNA PSFRSQISRS AQIWNSSVSN VRLAESSSGA
     DFAYYEGNDS RGSYASTDGH GSGYIFLDYR QNQQYDSTRV TAHETGHVLG LPDHYSGPCS
     ELMSGGGPGP SCTNPYPNST ERSRVNQLWA YGFQAALDKA LEKASQR