ID   NUC_STAAS               Reviewed;         228 AA.
AC   Q6GB41;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Thermonuclease;
DE            Short=TNase;
DE            EC=3.1.31.1;
DE   AltName: Full=Micrococcal nuclease;
DE   AltName: Full=Staphylococcal nuclease;
DE   Flags: Precursor;
GN   Name=nuc; OrderedLocusNames=SAS0756;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at
CC       the 5' position of the phosphodiester bond. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.31.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10048, ECO:0000255|PROSITE-
CC         ProRule:PRU10049};
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00272}.
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; BX571857; CAG42530.1; -; Genomic_DNA.
DR   RefSeq; WP_001793574.1; NC_002953.3.
DR   AlphaFoldDB; Q6GB41; -.
DR   BMRB; Q6GB41; -.
DR   SMR; Q6GB41; -.
DR   KEGG; sas:SAS0756; -.
DR   HOGENOM; CLU_046484_5_2_9; -.
DR   OMA; ISDGTHE; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 2.40.50.90; -; 1.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   InterPro; IPR002071; Thermonucl_AS.
DR   Pfam; PF00565; SNase; 1.
DR   SMART; SM00318; SNc; 1.
DR   SUPFAM; SSF50199; SSF50199; 1.
DR   PROSITE; PS01123; TNASE_1; 1.
DR   PROSITE; PS01284; TNASE_2; 1.
DR   PROSITE; PS50830; TNASE_3; 1.
PE   3: Inferred from homology;
KW   Calcium; Endonuclease; Hydrolase; Metal-binding; Nuclease; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..60
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000045235"
FT   CHAIN           61..228
FT                   /note="Thermonuclease"
FT                   /id="PRO_0000045236"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   228 AA;  25126 MW;  14DA80DB4FBD43FC CRC64;
     MTEYLLSAGI CMAIVSILLI GMAISNVSKG QYAKRFFFFA TSCLVLTLVV VSSLSSSANA
     SQTDNGVNRS GSEHPTVYSA TSTKKLHKEP ATLIKAIDGD TVKLMYKGQP MTFRLLLVDT
     PETKHPKKGV EKYGPEASAF TKKMVENAKK IEVEFDKGQR TDKYGRGLAY IYADGKMVNE
     ALVRQGLAKV AYVYKPNNTH EQLLRKSEAQ AKKEKLNIWS EDNADSGQ