ID   MUTS2_BACC1             Reviewed;         786 AA.
AC   Q72ZJ0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=BCE_4678;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43579.1; -; Genomic_DNA.
DR   RefSeq; WP_000893718.1; NC_003909.8.
DR   AlphaFoldDB; Q72ZJ0; -.
DR   SMR; Q72ZJ0; -.
DR   EnsemblBacteria; AAS43579; AAS43579; BCE_4678.
DR   GeneID; 59154865; -.
DR   KEGG; bca:BCE_4678; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000002527; 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..786
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075468"
FT   DOMAIN          711..786
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   786 AA;  88217 MW;  AE5389936EB09BA9 CRC64;
     MLERTLRVLE YNKVKEQLLE HTASSLGRDK VKHLVPSTDF EEIVEMQDTT DEAAKVIRLK
     GSAPLGGITD IRSNVKRAKI GSMLSPNELL DIANTMYGSR NMKRFIEDMV DNGVDLPILE
     THVAQIVSLY DLEKKITNCI GDGGEVVDSA SDKLRGIRTQ IRTAESRIRE KLENMTRSSN
     AQKMLSDSIV TIRNERYVIP VKQEYRGVYG GIVHDQSASG QTLFIEPQVI VELNNALQEA
     RVKEKQEIER ILLMLTEEVA VEADIVLSNV EVVANLDFIF AKAFYAKRIK ATKPIVNNER
     YMDLRQARHP LIDPEVIVPN NIMLGKDFTT IVITGPNTGG KTVTLKTVGI CVLMAQSGLH
     IPVMDESEIC VFKNIFADIG DEQSIEQSLS TFSSHMVNIV DILEKADFES LVLFDELGAG
     TDPQEGAALA ISILDEVCNR GARVVATTHY PELKAYGYNR EQVINASVEF DVNTLSPTYK
     LLIGVPGRSN AFEISKRLGL SDRVIEQARN HISTDTNKIE NMIAKLEESQ KNAERDWNEA
     EALRKQSEKL HRELQRQIIE FNEERDERLL KAQKEGEEKV EAAKKEAEGI IQELRQLRKA
     QLANVKDHEL IEAKSRLEGA APELVKKQKV NVKNTAPKQQ LRAGDEVKVL TFGQKGQLLE
     KVSDTEWSVQ IGILKMKVKE SDMEYINTPK QTEKKAVATV KGRDYHVSLE LDLRGERFEN
     AMARVEKYLD DAQLASYPRV SIIHGKGTGA LRQGVQDYLK KHRGVKTFRY GDMGEGGLGV
     TVVELK