ID   MUTS2_STAAU             Reviewed;         719 AA.
AC   Q9ZEH5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
DE   Flags: Fragment;
GN   Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; Synonyms=mutSB;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9144 / DSM 683 / NCIB 6571 / NCTC 6571 / NRRL B-314 / Oxford;
RA   Uziel O., Borovok I., Schreiber R., Cohen G., Aharonowitz Y.;
RT   "Transcriptional analysis of the thioredoxin (trxA) and thioredoxin
RT   reductase (trxB) genes in Staphylococcus aureus.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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; AJ223480; CAA11403.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZEH5; -.
DR   SMR; Q9ZEH5; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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.
FT   CHAIN           <1..719
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115232"
FT   DOMAIN          644..719
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         273..280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   NON_TER         1
SQ   SEQUENCE   719 AA;  81300 MW;  A427FF0796EB75CE CRC64;
     SLSGLSKVSA FIHRADIGGV LNVSELNLIK RLIQVQNQFK TFYNQLVEED EGVKYPILDD
     KMNQLPVLTD LFQQINETCD TYDLYDNASY ELQGIRSKIS STNQRIRQNL DRIVKSQANQ
     KKLSDAIVTV RNERNVIPVK AEYRQDFNGI VHDQSASGQT LYIEPSSVVE MNNQISRLRH
     DEAIEKERIL TQLTGYVAAD KDALLVAEQV MGQLDFLIAK ARYSRSIKGT KPIFKEERTV
     YLPKAYHPLL NRETVVANTI EFMEDIETVI ITGPNTGGKT VTLKTLGLII VMAQSGLLIP
     TLDGSQLSVF KNVYCDIGDE QSIEQSLSTF SSHMTNIVEI LKNADKHSLV LFDELGAGTD
     PSEGAALAMS ILDHVRKIGS LVMATTHYPE LKAYSYNREG VMNASVEFDV DTLSPTYKLL
     MGVPGRSNAF DISKKLGLSL NIINKAKTMI GTDEKEINEM IESLERNYKR VETQRLELDR
     LVKEAEQVHD DLSKQYQQFQ NYEKSLIEDA KEKANQKIKA ATKEADDIIK DLRQLREQKG
     ADVKEHELID KKKRLDDHYE AKSIKQNVQK QKYDKIVAGD EVKVLSYGQK GEVLEIVNDE
     EAIVQMGIIK MKLPIEDLEK KQKEKVKPTK MVTRQNRQTI KTELDLRGYR YEDALIELDQ
     YLDQAVLSNY EQVYIIHGKG TGALQKGVQQ HLKKHKSVSD FRGGMPSEGG FGVTVATLK