ID   MUTS2_STRT1             Reviewed;         783 AA.
AC   Q5LY40;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=str1762;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV63280.1; -; Genomic_DNA.
DR   RefSeq; WP_011227556.1; NC_006449.1.
DR   AlphaFoldDB; Q5LY40; -.
DR   SMR; Q5LY40; -.
DR   KEGG; stc:str1762; -.
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..783
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093405"
FT   DOMAIN          708..783
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   783 AA;  88024 MW;  187FFD9AB3C37D80 CRC64;
     MNTKILDQLE FNKVKDQFTE YLQTEQAQAE LCDLVPMTNP ERIQNQFTEI QEMSEIFVEH
     HGFAIGSLRD ISEPLRRLEL DADLNIQELI AIKKVLQASA DLSRFYADLE NVELIALKRL
     FEKIEAFPSL QGSLQSINDG GFIEHFASPE LQNIRRQLKA CDDAIRQTLQ DILKKSGHML
     AENLIASRNG RSVLPVKNTY RNRIAGVVHD ISSSGNTVYI EPRAVIQLNE KITQLRADER
     HEMARILHEL SDQLRPHTAA IANNAWILGH MDFIRGKYLY LHDKKAIIPE ISDNQTLQLL
     NVRHPLLINP VANDLRFDED LTVIVITGPN TGGKTVMLKT LGLAQLMAQS GLPILADKGS
     RVAIFQEIFA DIGDEQSIEQ SLSTFSSHMT HIVEILNTAD SNSLVLVDEL GAGTDPQEGA
     SLAMAILEHL RLSQIKTMAT THYPELKAYG IETQHVENAS MEFDTATLRP TYRFMQGVPG
     RSNAFEIARR LGLNEIIVKE AENLTDTDSD VNRIIEQLEA QTVETQKRLE HIKDVEQENL
     KFNRAVKKLY NEFSHEYDKE LEKAQKEIQE MVDTALAESD SILKNLHDKS QLKPHEVIDA
     KGKLKKLAAQ VDLSKNKVLR KAKKEKAARA PRVGDDIIVT AYGQRGTLTS QAKNGNWEAQ
     VGLIKMSLKA DEFTLVRTQA EAQQPKKKQI NVVKKAKKTS SDGPRARLDL RGKRYEEAMQ
     ELDAFIDQAL LNNMSQVEII HGIGTGVIRD AVTKYLRRHR HVKNFEYAPQ SAGGSGCTIA
     TLG