ID   MUTS2_STREM             Reviewed;         778 AA.
AC   B4U143;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Sez_0334;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(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; CP001129; ACG61710.1; -; Genomic_DNA.
DR   RefSeq; WP_012514989.1; NC_011134.1.
DR   AlphaFoldDB; B4U143; -.
DR   SMR; B4U143; -.
DR   EnsemblBacteria; ACG61710; ACG61710; Sez_0334.
DR   KEGG; sez:Sez_0334; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001873; 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..778
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093389"
FT   DOMAIN          703..778
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   778 AA;  87173 MW;  B3BA0F020A0DD600 CRC64;
     MEKKILEQLE FEKVKEQFWP YLQTEQGQLE LDLLEPIANK DKIQAYFTEL EEMAAIFVEH
     HHFALGGLSD VSESMQRLDL EADLSIQELL EVKKLLQVSA EACRFYADLE NVDLVALKAL
     FEKIESFPSL QGSLQAINDA GFVEGFASPE LESIRRQISN KEHASRQLLQ DILKKQAAYL
     SESLIASRNG RSVLPVKNTY RHKVAGVVHD MSASGSTVYI EPRALVSLNE ELTQLQTDER
     HEIGRILHEL SEQLRPHSRS LRNNAWLLGH LDLVRAKYLY MQAKQAAVPV ISDDKSLQLL
     NARHPLIQNP VANDLHFAND LAVIVITGPN TGGKTIMLKT LGLAQVMAQS GLPILADKGS
     RVAVFNGIYA DIGDEQSIEQ SLSTFSSHMT HIVEILKQAD SDSLILFDEL GAGTDPQEGA
     SLAMAILEQL RLTNIKTMAT THYPELKAYG IETAYVENAS MAFDNVSLKP TYRFMQGVPG
     RSNAFDIARR LGLAEHIVKE AQAMTATNHD VNRIIEQLEQ QTLESRKRLE HIKEVEQDNL
     KFNRAVKKLY NEFSHAKDKE LEKAALEARE IVDMALAESE SILSQLHEKA ELKPHEIIEA
     KHRLKQLVPE QSLSQNKVLK KAKKWRAPRV GDDIIVTAYG QRGTLLAQLK DKRWEAQVGL
     IKLTLKEDEF SLVKLKEEAQ QPKKRAVKVV KKAATGKGPR ARLDLRGKRY EEAMQELDAF
     IDQALLNNMS QVDIIHGIGT GVIREAVGKY LRRNKHVKSF GYAPQNAGGS GCTIANLG