ID   MUTS2_STRU0             Reviewed;         777 AA.
AC   B9DVK7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SUB1560;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(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; AM946015; CAR43343.1; -; Genomic_DNA.
DR   RefSeq; WP_015911866.1; NC_012004.1.
DR   AlphaFoldDB; B9DVK7; -.
DR   SMR; B9DVK7; -.
DR   STRING; 218495.SUB1560; -.
DR   PRIDE; B9DVK7; -.
DR   EnsemblBacteria; CAR43343; CAR43343; SUB1560.
DR   KEGG; sub:SUB1560; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000449; 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_1000118569"
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;  87925 MW;  A637C7A0CA9DBF58 CRC64;
     MNQKILEQLE FQKVKEQFQP YLQTAQGIQE LRLLEPSNHY DKISDYFKEI AEMATIFVEN
     HHFSIGNLRD VSESMRRLEL EADLNIQELL DIKKLLLVSG EISRFYQDLE NVDLQVLKRI
     FEKIEVFPQL QGSLQAVNDA AFIENFASPE LDRLRRQIAE NERYSRQLLQ DILKKNADYL
     SESLIASRNG KSVLPVKNTF RHRVSGVVHD ISASGNTVYI EPRALVQVNE EMTQLLADER
     HEIARILKEL SQLLRPHSRA LANNAWLLGH LDFVRAKYHY LVNNKATIPK ISKDKNIQLL
     NVRHPLLKNP VANDLHFADD LAVIVITGPN TGGKTIMLKT LGLAQLMGQS GLPILADEGS
     KIAVFDAIYA DIGDEQSIEQ SLSTFSSHMT HIVDILEESN SNSLVLFDEL GAGTDPQEGA
     SLAMAILEQL RLTNIKTMAT THYPELKAYG IESDYVENAS MEFDSQSLKP TYRFMQGVPG
     RSNAFEIARR LGLAETIVKE AEQMTDTDSD VNRIIEELER QTLSSRRRLD HIREVEQENI
     KFNRAVKKLY NEFSLAKDKE IEKASQEAQA IVELALTESE EILSKLHEKA ELKPHEIIEA
     KSKLKSLVPQ RDLSKNKVLK KAKKLREPRI GDDIIVSAYG QRGTLIGQVK GNKWEAQVGL
     IKMTLKEDEF QLVKVEAEAQ KPKKQSINMV KKANQNGPRA RLDLRGKRYE EAMQELDAFI
     DQALVNNMSQ VDIIHGIGTG VIREAVTKYL RRHKHVKSFA YAPQNAGGSG CTIATLG