NUC_STAAC
ID NUC_STAAC Reviewed; 228 AA.
AC Q5HHM4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SACOL0860;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36415.1; -; Genomic_DNA.
DR RefSeq; WP_001548082.1; NC_002951.2.
DR PDB; 4WRD; X-ray; 1.65 A; A=80-228.
DR PDB; 5DAU; X-ray; 1.50 A; A=80-228.
DR PDBsum; 4WRD; -.
DR PDBsum; 5DAU; -.
DR AlphaFoldDB; Q5HHM4; -.
DR BMRB; Q5HHM4; -.
DR SMR; Q5HHM4; -.
DR EnsemblBacteria; AAW36415; AAW36415; SACOL0860.
DR KEGG; sac:SACOL0860; -.
DR HOGENOM; CLU_046484_5_2_9; -.
DR OMA; ISDGTHE; -.
DR Proteomes; UP000000530; 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_0000045227"
FT CHAIN 61..228
FT /note="Thermonuclease"
FT /id="PRO_0000045228"
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"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4WRD"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4WRD"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4WRD"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:4WRD"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:4WRD"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4WRD"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:4WRD"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4WRD"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:4WRD"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4WRD"
SQ SEQUENCE 228 AA; 25120 MW; 1505918EA02F1273 CRC64;
MTEYLLSAGI CMAIVSILLI GMAISNVSKG QYAKRFFYFA TSCLVLTLVV VSSLSSSANA
SQTDNGVNRS GSEDPTVYSA TSTKKLHKEP ATLIKAIDGD TVKLMYKGQP MTFRLLLVDT
PETKHPKKGV EKYGPEASAF TKKMVENAKK IEVEFDKGQR TDKYGRGLAY IYADGKMVNE
ALVRQGLAKV AYVYKPNNTH EQLLRKSEAQ AKKEKLNIWS EDNADSGQ
