NUC_STAAR
ID NUC_STAAR Reviewed; 228 AA.
AC Q6GIK1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-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=SAR0847;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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}.
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DR EMBL; BX571856; CAG39855.1; -; Genomic_DNA.
DR RefSeq; WP_001643461.1; NC_002952.2.
DR AlphaFoldDB; Q6GIK1; -.
DR BMRB; Q6GIK1; -.
DR SMR; Q6GIK1; -.
DR KEGG; sar:SAR0847; -.
DR HOGENOM; CLU_046484_5_2_9; -.
DR OMA; ISDGTHE; -.
DR OrthoDB; 1719840at2; -.
DR Proteomes; UP000000596; 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_0000045233"
FT CHAIN 61..228
FT /note="Thermonuclease"
FT /id="PRO_0000045234"
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; 25196 MW; 73F150066DEF0B5C CRC64;
MTEYLLSAGI CMAIVSILLI GMAISNVSKE QYAKRFFFFA TSCLVLTLVV ASSLSSSANA
SQTDNGVNRS GSEYPTVYSA TSTKKLHKEP ATLIKAIDGD TVKLMYKGQP MTFRLLLVDT
PETKHPKKGV EKYGPEASAF TKKMVENAKK IEVEFDKGQR TDKYGRGLAY IYADGKMVNE
ALVRQGLAKV AYVYKPNNTH EQLLRKSEAQ AKKEKLNIWS EDNADSGQ