NUC_STAAW
ID NUC_STAAW Reviewed; 228 AA.
AC Q8NXI6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MW0769;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94634.1; -; Genomic_DNA.
DR RefSeq; WP_001793574.1; NC_003923.1.
DR PDB; 2LKV; NMR; -; A=80-228.
DR PDB; 2M00; NMR; -; A=80-228.
DR PDB; 2OXP; X-ray; 2.00 A; A=80-228.
DR PDB; 2PW5; X-ray; 2.10 A; A=80-228.
DR PDB; 2PW7; X-ray; 2.10 A; A=80-228.
DR PDB; 2PYK; X-ray; 2.10 A; A=80-228.
DR PDB; 2PZT; X-ray; 2.10 A; A=80-228.
DR PDB; 2PZU; X-ray; 2.10 A; A=80-228.
DR PDB; 2PZW; X-ray; 2.10 A; A=80-228.
DR PDB; 3D4W; X-ray; 1.90 A; A=80-228.
DR PDB; 3D8G; X-ray; 1.99 A; A=80-228.
DR PDB; 3MVV; X-ray; 1.72 A; A=80-228.
DR PDB; 3QOJ; X-ray; 1.60 A; A=80-228.
DR PDB; 3QOL; X-ray; 1.90 A; A=80-228.
DR PDB; 3R3O; X-ray; 1.90 A; A=80-228.
DR PDB; 6AMF; X-ray; 1.85 A; A=80-228.
DR PDBsum; 2LKV; -.
DR PDBsum; 2M00; -.
DR PDBsum; 2OXP; -.
DR PDBsum; 2PW5; -.
DR PDBsum; 2PW7; -.
DR PDBsum; 2PYK; -.
DR PDBsum; 2PZT; -.
DR PDBsum; 2PZU; -.
DR PDBsum; 2PZW; -.
DR PDBsum; 3D4W; -.
DR PDBsum; 3D8G; -.
DR PDBsum; 3MVV; -.
DR PDBsum; 3QOJ; -.
DR PDBsum; 3QOL; -.
DR PDBsum; 3R3O; -.
DR PDBsum; 6AMF; -.
DR AlphaFoldDB; Q8NXI6; -.
DR BMRB; Q8NXI6; -.
DR SMR; Q8NXI6; -.
DR EnsemblBacteria; BAB94634; BAB94634; BAB94634.
DR KEGG; sam:MW0769; -.
DR HOGENOM; CLU_046484_5_2_9; -.
DR OMA; ISDGTHE; -.
DR EvolutionaryTrace; Q8NXI6; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..60
FT /evidence="ECO:0000250"
FT /id="PRO_0000045237"
FT CHAIN 61..228
FT /note="Thermonuclease"
FT /id="PRO_0000045238"
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"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2M00"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2LKV"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2LKV"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2LKV"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3QOJ"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3QOJ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3QOJ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3D8G"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:3QOJ"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3QOJ"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2M00"
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
