ID   NUC_STAAN               Reviewed;         228 AA.
AC   Q7A6P2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=SA0746;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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}.
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DR   EMBL; BA000018; BAB41979.1; -; Genomic_DNA.
DR   PIR; H89852; H89852.
DR   RefSeq; WP_000141557.1; NC_002745.2.
DR   AlphaFoldDB; Q7A6P2; -.
DR   BMRB; Q7A6P2; -.
DR   SMR; Q7A6P2; -.
DR   EnsemblBacteria; BAB41979; BAB41979; BAB41979.
DR   KEGG; sau:SA0746; -.
DR   HOGENOM; CLU_046484_5_2_9; -.
DR   OMA; ISDGTHE; -.
DR   BRENDA; 3.1.31.1; 3352.
DR   Proteomes; UP000000751; Chromosome.
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_0000045231"
FT   CHAIN           61..228
FT                   /note="Thermonuclease"
FT                   /id="PRO_0000045232"
FT   REGION          58..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  25090 MW;  6F288E1F368D8FF8 CRC64;
     MTEYLLSAGI CMAIVSILLI GMAISNVSKG QYAKRFFFFA TSCLVLTLVV VSSLSSSANA
     SQTDNGVNRS GSEDPTVYSA TSTKKLHKEP ATLIKAIDGD TVKLMYKGQP MTFRLLLVDT
     PETKHPKKGV EKYGPEASAF TKKMVENANK IEVEFDKGQR TDKYGRGLAY IYADGKMVNE
     ALVRQGLAKV AYVYKPNNTH EQLLRKSEAQ AKKEKLNIWS EDNADSGQ