ID   MUTS2_BACCZ             Reviewed;         786 AA.
AC   Q633P2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BCE33L4296;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU15973.1; -; Genomic_DNA.
DR   RefSeq; WP_000893731.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q633P2; -.
DR   SMR; Q633P2; -.
DR   EnsemblBacteria; AAU15973; AAU15973; BCE33L4296.
DR   KEGG; bcz:BCE33L4296; -.
DR   PATRIC; fig|288681.22.peg.1080; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000002612; 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_1000075470"
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;  88216 MW;  673334742C314A74 CRC64;
     MLERTLRVLE YNKVKEQLLE HTASSLGRDK VKHLVPSTDF EEIVEMQDTT DEAAKVIRLK
     GSAPLGGITD IRSNVKRAKI GSMLSPNELL DIANTMYGSR NMKRFIEDMV DNGVELPILE
     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 SDRVIDQARN HISTDTNKIE NMIAKLEESQ KNAERDWNEA
     EALRKQSEKL HRELQRQIIE FNEERDERLL KAQKEGEEKV EAAKKEAEGI IQELRQLRKA
     QLANVKDHEL IEAKSRLEGA APELVKKQKV NVKNTAPKQQ LRAGDEVKVL TFGQKGQLLE
     KVSDTEWSVQ IGILKMKVKE SNMEYINTPK QTEKKAVATV KGRDYHVSLE LDLRGERFEN
     AMARVEKYLD DAQLASYPRV SIIHGKGTGA LRQGVQDYLK KHRGVKTFRY GDMGEGGLGV
     TVVELK