ID   MUTS2_STRE4             Reviewed;         778 AA.
AC   C0MAV6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SEQ_0399;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW92550.1; -; Genomic_DNA.
DR   RefSeq; WP_012679025.1; NC_012471.1.
DR   AlphaFoldDB; C0MAV6; -.
DR   SMR; C0MAV6; -.
DR   EnsemblBacteria; CAW92550; CAW92550; SEQ_0399.
DR   KEGG; seu:SEQ_0399; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001365; 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   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_1000118566"
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;  87100 MW;  2E6EF4346017D612 CRC64;
     MEKKILEQLE FEKVKEQFWP YLQTEQGQLE LDLLEPIANK DKIQAYFTEL EEMAAIFVEH
     HHFALGGLSD VSESMQRLDL EADLSIQELL AVKKLLQVSA EVCRFYADLE NVDLVALKAL
     FEKIESFPSL QGSLQAINDA GFVEGFASPE LESIRRQISN KEHASRQLLQ DILKKQAAYL
     SESLIASRNG RSVLPVKNTY RHKVAGVVHD MSASGSTVYI EPRALVSLNE ELTQLQTDER
     HEIGRILHEL SEQLRPHSRS LRNNAWLLGH LDLVRAKYLY MQAKQATVPV ISDDKSLQLL
     NARHPLIQNP VANDLHFAND LAVIVITGPN TGGKTIMLKT LGLAQVMAQS GLPILADKGS
     RVAVFNGIYA DIGDEQSIEQ SLSTFSSHMT HIVEILNQAD SDSLILFDEL GAGTDPQEGA
     SLAMAILEQL RLTNIKTMAT THYPELKAYG IETAYVENAS MAFDNVSLKP TYRFMQGVPG
     RSNAFDIARR LGLAEHIVKE AQAMTATDHD VNRIIEQLEQ QTLESRKRLE HIKEVEQDNL
     KFNRAVKKLY NEFSHAKDKE LEKAALEARE IVDIALAESD SILSQLHEKA ELKPHEIIEA
     KHRLKQLAPE QSLSQNKVLK KAKKWRAPRV GDDIIVTAYG QRGTLLAQLK DKRWEAQVGL
     IKLTLKEDEF SLVKLKEEAQ QPKKRAVKVV KKAATGKGPR ARLDLRGKRY EEAMQELDAF
     IDQALLNNMS QVDIIHGIGT GVIREAVGKY LRRNKHVKSF GYAPQNAGGS GCTIANLG