ID   MUTS2_STAA8             Reviewed;         782 AA.
AC   Q2FZD3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
GN   OrderedLocusNames=SAOUHSC_01099;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- FUNCTION: Endonuclease that is involved in the suppression of
CC       homologous recombination and may therefore have a key role in the
CC       control of bacterial genetic diversity. {ECO:0000255|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR   EMBL; CP000253; ABD30213.1; -; Genomic_DNA.
DR   RefSeq; WP_001249285.1; NZ_LS483365.1.
DR   RefSeq; YP_499643.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZD3; -.
DR   SMR; Q2FZD3; -.
DR   STRING; 1280.SAXN108_1139; -.
DR   EnsemblBacteria; ABD30213; ABD30213; SAOUHSC_01099.
DR   GeneID; 3920741; -.
DR   KEGG; sao:SAOUHSC_01099; -.
DR   PATRIC; fig|93061.5.peg.1007; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   PRO; PR:Q2FZD3; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro.
DR   CDD; cd03280; ABC_MutS2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00092; MutS2; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   PANTHER; PTHR11361:SF14; PTHR11361:SF14; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF01713; Smr; 1.
DR   PIRSF; PIRSF005814; MutS_YshD; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01069; mutS2; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..782
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093380"
FT   DOMAIN          707..782
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         336..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   782 AA;  88661 MW;  1DFC2347703100EA CRC64;
     MRQKTLDVLE FEKIKSLVAN ETISDLGLEK VNQMMPATNF ETVVFQMEET DEIAQIYNKH
     RLPSLSGLSK VSAFIHRADI GGVLNVSELN LIKRLIQVQN QFKTFYNQLV EEDEGVKYPI
     LDDKMNQLPV LTDLFQQINE TCDTYDLYDN ASYELQGIRS KISSTNQRIR QNLDRIVKSQ
     ANQKKLSDAI VTVRNERNVI PVKAEYRQDF NGIVHDQSAS GQTLYIEPSS VVEMNNQISR
     LRHDEAIEKE RILTQLTGYV AADKDALLVA EQVMGQLDFL IAKARYSRSI KGTKPIFKED
     RTVYLPKAYH PLLNRETVVA NTIEFMEDIE TVIITGPNTG GKTVTLKTLG LIIVMAQSGL
     LIPTLDGSQL SVFKNVYCDI GDEQSIEQSL STFSSHMTNI VEILKHADKH SLVLFDELGA
     GTDPSEGAAL AMSILDHVRK IGSLVMATTH YPELKAYSYN REGVMNASVE FDVDTLSPTY
     KLLMGVPGRS NAFDISKKLG LSLNIINKAK TMIGTDEKEI NEMIESLERN YKRVETQRLE
     LDRLVKEAEQ VHDDLSKQYQ QFQNYEKSLI EEAKEKANQK IKAATKEADD IIKDLRQLRE
     QKGADVKEHE LIDKKKRLDD HYEAKSIKQN VQKQKYDKIV AGDEVKVLSY GQKGEVLEIV
     NDEEAIVQMG IIKMKLPIED LEKKQKEKVK PTKMVTRQNR QTIKTELDLR GYRYEDALIE
     LDQYLDQAVL SNYEQVYIIH GKGTGALQKG VQQHLKKHKS VSDFRGGMPS EGGFGVTVAT
     LK