ID   MUTS2_STRPG             Reviewed;         779 AA.
AC   A2RCQ8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; OrderedLocusNames=SpyM50289;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
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; AM295007; CAM29631.1; -; Genomic_DNA.
DR   RefSeq; WP_011888615.1; NC_009332.1.
DR   AlphaFoldDB; A2RCQ8; -.
DR   SMR; A2RCQ8; -.
DR   KEGG; spf:SpyM50289; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
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_1000093396"
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;  87840 MW;  0AF7255B1BE8E3AF CRC64;
     MNNKILEQLE FNKVKELLLP YLKTEQSQEE LLELEPMTEA SKIEKSFNEI SDMEQIFVEH
     HSFGIVSLSS ISESLKRLEL SADLNIQELL AIKKVLQSSS DMIHFYSDLD NVSFQSLDRL
     FENLEQFPNL QGSFQAINDG GFLEHFASPE LERIRRQLTN SERRVRQILQ DMLKEKAELL
     SENLIASRSG RSVLPVKNTY RNRISGVVHD ISSSGSTVYI EPRAVVTLNE EITQLRADER
     HEEGRILHAF SDLLRPHVAT IRNNAWILGH LDFVRAKYLF MSDNKATIPK ISNDSTLALI
     NVRHPLLSNP VANDLHFDHD LTAIVITGPN TGGKTIMLKT LGLAQLMGQS GLPVLADKGS
     KIAVFNNIFA DIGDEQSIEQ SLSTFSSHMT HIVSILNEAD HNSLVLFDEL 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
     VGIIKMTLTH DEFTLVRVQE EQKVKNKQIN VVKKADSSGP RARLDLRGKR YEEAMQELDH
     FIDQALLNNM GQVDIIHGIG TGVIREGVTK YLRRHKHVKH FAYAPQNAGG SGATIVTLG