ID   MUTS2_STRSV             Reviewed;         777 AA.
AC   A3CKV4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SSA_0355;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(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; CP000387; ABN43809.1; -; Genomic_DNA.
DR   RefSeq; WP_011836455.1; NC_009009.1.
DR   RefSeq; YP_001034359.1; NC_009009.1.
DR   AlphaFoldDB; A3CKV4; -.
DR   SMR; A3CKV4; -.
DR   STRING; 388919.SSA_0355; -.
DR   EnsemblBacteria; ABN43809; ABN43809; SSA_0355.
DR   KEGG; ssa:SSA_0355; -.
DR   PATRIC; fig|388919.9.peg.342; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000002148; 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..777
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093403"
FT   DOMAIN          702..777
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   777 AA;  87398 MW;  A6A1802C96EE8F3D CRC64;
     MNTKILETLE FSKIKELFAP YLLTEQGQLE LGLLLPTSKK ETVVSAFLEM TDMQQIFVQH
     PHFSLAATQD ITALTKRLEL ESDLNIEEFL ALKRVLAVTQ ELKSFYEDLE NVHLEKLDRL
     FDNLAVFPKL QGSLQAVNDG GFIESFASES LSRIRRKIQE NENQVREILQ EILKNKGEML
     ADQVVASRNG RNVLPVKNTY RNRISGVVHD ISASGNTVYI EPRAVVNLNE EIASSRADER
     YEIQRILQEL SDLFRPHAAE IANNAWIIGH LDLVRAKVRF MQETGAVVPD LSEEQDIQLL
     SVRHPLIENA VANDLHFGLD LTEIVITGPN TGGKTIMLKT LGLAQIMAQS GLPILADKGS
     RVGIFSQIFA DIGDEQSIEQ SLSTFSSHMT NIVSILEQVD SESLVLLDEL GAGTDPQEGA
     ALAIAILEDL RLRQIKTMAT THYPELKAYG IETDWVENAS MEFDTDSLRP TYRFMQGVPG
     RSNAFEIAQR LGLSEVIVGH AQEQTDTDSD VNRIIERLEE QTLESRKRLD NIREVEQENL
     KFNRALKKLY NEFNREKETE LNKARLEAQE IVDLALSESE SILKNLHDKS SLKPHEIIEA
     KAQLKKLAPE TVDLSKNKVL KQAKKNRAPK VGDDILVTSY GQRGTLVKQL KDGRWEAQVG
     LIKMTLEEQE FNLLKAEKEQ QPKRKQVNVV KRANTAGPKA RLDLRGKRYE EAMEELDAFI
     DQALLNNMAQ VDIIHGIGTG VIREGVTKYL RRNKHVKSFG YAPQNAGGSG ATIVIFK