ID SNPA2_STRLI Reviewed; 227 AA.
AC P0A3Z8; P43162;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 13-SEP-2023, entry version 67.
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;
OS Streptomyces lividans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=66 / 1326;
RX PubMed=1464066; DOI=10.1139/m92-148;
RA Butler M.J., Davey C.C., Krygsman P., Walczyk E., Malek L.T.;
RT "Cloning of genetic loci involved in endoprotease activity in Streptomyces
RT lividans 66: a novel neutral protease gene with an adjacent divergent
RT putative regulatory gene.";
RL Can. J. Microbiol. 38:912-920(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 113-131.
RC STRAIN=TK24;
RX PubMed=1547948; DOI=10.1016/0378-1119(92)90613-t;
RA Lichenstein H.S., Busse L.A., Smith G.A., Narhi L.O., McGinley M.O.,
RA Rohde M.F., Katzowitz J.L., Zukowski M.M.;
RT "Cloning and characterization of a gene encoding extracellular
RT metalloprotease from Streptomyces lividans.";
RL Gene 111:125-130(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Takahashi H.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase M7 family. {ECO:0000305}.
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DR EMBL; M81703; AAA26740.1; -; Genomic_DNA.
DR EMBL; M89476; AAA26805.1; -; Genomic_DNA.
DR EMBL; D00670; BAA00573.1; -; Genomic_DNA.
DR PIR; JH0571; JH0571.
DR AlphaFoldDB; P0A3Z8; -.
DR SMR; P0A3Z8; -.
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; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR000013; Peptidase_M7.
DR NCBIfam; NF033628; snapalysin; 1.
DR Pfam; PF02031; Peptidase_M7; 1.
DR PIRSF; PIRSF016573; Peptidase_M7; 1.
DR PRINTS; PR00787; NEUTRALPTASE.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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..29
FT /evidence="ECO:0000255"
FT PROPEP 30..42
FT /evidence="ECO:0000255"
FT /id="PRO_0000028648"
FT CHAIN 43..227
FT /note="Extracellular small neutral protease"
FT /id="PRO_0000028649"
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"
FT CONFLICT 210
FT /note="A -> R (in Ref. 3; BAA00573)"
FT /evidence="ECO:0000305"
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
//
