ID   MUTS2_STRP1             Reviewed;         779 AA.
AC   Q99Y73; Q48WU6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
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=SPy_1837, M5005_Spy1561;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34559.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52179.1; -; Genomic_DNA.
DR   RefSeq; NP_269838.1; NC_002737.2.
DR   AlphaFoldDB; Q99Y73; -.
DR   SMR; Q99Y73; -.
DR   STRING; 1314.HKU360_01683; -.
DR   PaxDb; Q99Y73; -.
DR   EnsemblBacteria; AAK34559; AAK34559; SPy_1837.
DR   KEGG; spy:SPy_1837; -.
DR   KEGG; spz:M5005_Spy1561; -.
DR   PATRIC; fig|160490.10.peg.1596; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000750; 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; Reference proteome.
FT   CHAIN           1..779
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093392"
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;  87804 MW;  F99E2C47EE5A4473 CRC64;
     MNNKILEQLE FNKVKELLLP YLKTEQSQEE LLELEPMTEA PKIEKSFNEI SDMEQIFVEH
     HSFGIVSLSS ISESLKRLEL STDLNIQELL 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
     VGIIKMTLTQ DEFSLVRVQE EQKVKNKQIN VVKKADGSGP RARLDLRGKR YEEAMQELDH
     FIDQALLNNM GQVDIIHGIG TGVIREGVTK YLRRNKHVKH FAYAPQNAGG SGATIVTLG