ID   MUTS2_STRPZ             Reviewed;         779 AA.
AC   B5XI46;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Spy49_1434c;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
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; CP000829; ACI61708.1; -; Genomic_DNA.
DR   RefSeq; WP_012560934.1; NC_011375.1.
DR   AlphaFoldDB; B5XI46; -.
DR   SMR; B5XI46; -.
DR   EnsemblBacteria; ACI61708; ACI61708; Spy49_1434c.
DR   KEGG; soz:Spy49_1434c; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001039; 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: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.
FT   CHAIN           1..779
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093400"
FT   DOMAIN          704..779
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         328..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   779 AA;  87947 MW;  246AB3B4A77EE31C CRC64;
     MNNKILEQLE FNKVKELLLP YLKTEQSQEE LLELEPMTEA PKIEKSFNEI SDMEQIFVEH
     HSFGIVSLSS ISESLKRLEL SADLNIQELL AIKKVLQSSS DMIHFYSDLN NISFQSLDRL
     FENLEQFPNL QGSFQAINDG GFLEHFASPE LERIRRQLTN SERRVRQILQ DMLKEKAELL
     SENLIASRSG RSVLPVKNTY RNRISGVVHD ISSSGTTVYI EPRAVVTLNE EITQLRADER
     HEEGRILHAF SDLLRPHVAT IRNNAWILGH LDFVRAKYLF MSDNKATIPK ISNDSTLVLI
     NVRHPLLSNP VANDLHFDHD LTAIVITGPN TGGKTIMLKT LGLAQLMGQS GLPVLADKGS
     KITVFNNIFA DIGDEQSIEQ SLSTFSSHMT HIVSILNEAD RNSLVLFDEL GAGTDPQEGA
     SLAMAILEHL RLSHIKTMAT THYPELKAYG IETNFVENAS MEFDAETLSP TYRFMQGVPG
     RSNAFEIASR LGLAPFIVKQ AKQMTDSDSD VNRIIEQLEA QTLETRRRLD HIKEVEQENL
     KFNRAVKKLY NEFSHERDKE LEKIYQEAQE IVDMALNESD TILKKLNDKS QLKPHEIIDA
     KAQIKKLAPQ VDLSKNKVLN KAKKIKAARA PRIGDDIIVT SYGQRGTLTS QLKDGRWEAQ
     VGIIKMTLTQ DEFSLVRVQE EQKVKNKQIN VVKKADSSGP RARLDLRGKR YEEAMQELDH
     FIDQSLLNNM GQVDIIHGIG TGVIREGVTK YLRRHKHVKH FAYAPQNAGG SGATIVTLG