ID   MUTS2_STRMU             Reviewed;         776 AA.
AC   Q8DSD1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=SMU_1870;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59487.1; -; Genomic_DNA.
DR   RefSeq; NP_722181.1; NC_004350.2.
DR   RefSeq; WP_002263362.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSD1; -.
DR   SMR; Q8DSD1; -.
DR   STRING; 210007.SMU_1870; -.
DR   PRIDE; Q8DSD1; -.
DR   EnsemblBacteria; AAN59487; AAN59487; SMU_1870.
DR   KEGG; smu:SMU_1870; -.
DR   PATRIC; fig|210007.7.peg.1666; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; Q8DSD1; -.
DR   Proteomes; UP000002512; 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..776
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093391"
FT   DOMAIN          701..776
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   776 AA;  87764 MW;  58D0908BD1A50B32 CRC64;
     MNTKILKALE FDKVKKQFTH FLQSEQGQME LNDLLPMTNQ EKIERSFAEI ADVAQIFQEY
     ASFGFGHSQD ISESLRRLEL GADLNTQELL AVKRILQMSA ELKDFYDNLE NVDLQILDCL
     FEKIETFPDL QGSLQAINDG GFIEDFASPE LTKIRHHIHQ NEQQIRQILQ EMLKKQGDLL
     AENLIASRSG RSVLPVKNTY RHRIAGVIHD ISASGNTVYI EPRAVVNLNE EMTQARADER
     HEMTRILHDL SDRLRSQTDI IGNNAWLLGH IDFVRGKYLY MRENQASLPS LTTDQTIRLL
     SVRHPLLSNP IANDLHFEHD TTAILITGPN TGGKTIMLKT LGITQLMAQS GLPILADEGS
     KVAVFKDIFA DIGDEQSIEQ SLSTFSSHMT HIVEILQKAN KDSLVLFDEL GAGTDPQEGA
     ALAMSILEHL RLSDIKTMIT THYPELKAYG IETEFIENAS MEFDMVTLSP TYHFMQGVPG
     RSNAFEIARR LGLSEIIVAE AENLTNTDSD VNKIIERLEN QTIESRRRLD NIREVEQENL
     KFNRAVKKLY NEFSHAQDKE LRKAKLKAQE IVDKALAESD FILKNLQDKA QLKPHEIIEA
     KGKLKKLVPE IELSKNKVLK KAKKKRAAKV GDDIIVSSYG QRGTLTKRFK DGRWEAQVGL
     IKMTLQESEF DLVKSDKAQA SQKRQAHLVK RTSQKAPSAR LDLRGKRYEE AMQELDEFID
     QALLNNMAQV DIIHGIGTGV IRDGVTKYLR RNKQVKEFGY APQNAGGSGA TIVTFK