ID   MUTS2_BACCN             Reviewed;         786 AA.
AC   A7GTK1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
GN   OrderedLocusNames=Bcer98_3240;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23459.1; -; Genomic_DNA.
DR   RefSeq; WP_012095698.1; NC_009674.1.
DR   AlphaFoldDB; A7GTK1; -.
DR   SMR; A7GTK1; -.
DR   STRING; 315749.Bcer98_3240; -.
DR   EnsemblBacteria; ABS23459; ABS23459; Bcer98_3240.
DR   GeneID; 56418783; -.
DR   KEGG; bcy:Bcer98_3240; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000002300; 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_1000075469"
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;  88517 MW;  FA1A140CC27D1242 CRC64;
     MLERTLRVLE YDKVKEQLLE HTASSLGRDK VKRLMPSTDF EEIVEMQDTT DEAAKVIRLK
     GHAPLGGIFD IRSNVKRAKI GSMLSPHELL DIASTMYGSR QMKRFIEDIV DNGAQLPILE
     THVAQIVSLY DLEKKITGCI GDGGEVLDSA SDKLRGIRNQ IRTAESRIRE KLENMTRSSN
     AQKMLSDAIV TIRNDRYVIP VKQEYRGVYG GIVHDQSASG QTLFIEPQVI VELNNALQEA
     RVKEKQEVER ILMMLTEEVA AEADIVLANV EVIANLDFIF AKALYAKRMK ATKPIVNNER
     YMELRQARHP LIDPKVIVPN DIVLGKDFTT IVITGPNTGG KTVTLKTVGI CVLMAQSGLH
     IPVQEESEIC VFKNIFADIG DEQSIEQSLS TFSSHMVNIV DILEKADFES LVLFDELGAG
     TDPQEGAALA ISILDEVHNR GARVVATTHY PELKAYGYNR NQVINASVEF DVNTLSPTYK
     LLIGVPGRSN AFEISKRLGL SERVINRARN HISTDTNKIE NMIAKLEESQ KNAERDWKEA
     EELRKQSEKL HRELQRQIIE FNEERDERLL KAQKEGEEKV EAAKKEAEAI IRELRQLRKA
     QLANVKDHEL IEAKSRLEGA APELVKKQKV KVKNTAPKQQ LRPGDEVKVL TFGQKGQLLK
     KVSDSEWNVQ IGILKMKVKE SDMEYINTPK QLEKKAVATV KGRDYHVSLE LDLRGERFEN
     AMMRVEKYLD DAQLANYPRV SIIHGKGTGA LRQGVQDYLK NHRGVKSFRY GDMGEGGLGV
     TVVELK