ID   MUTS2_OCEIH             Reviewed;         782 AA.
AC   Q8EPI1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=OB2124;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(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; BA000028; BAC14080.1; -; Genomic_DNA.
DR   RefSeq; WP_011066518.1; NC_004193.1.
DR   AlphaFoldDB; Q8EPI1; -.
DR   SMR; Q8EPI1; -.
DR   STRING; 221109.22777809; -.
DR   EnsemblBacteria; BAC14080; BAC14080; BAC14080.
DR   KEGG; oih:OB2124; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   PhylomeDB; Q8EPI1; -.
DR   Proteomes; UP000000822; 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..782
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075479"
FT   DOMAIN          707..782
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         331..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   782 AA;  87509 MW;  5C3EE2CBF8647329 CRC64;
     MNERVLRVLD FKSVTEMLKG QAETALGKER AKITKPLSSL DKINMLQDET DEAAKIIRLN
     QAIPLGGITD IRASVKRSSI GGILSTDECL DVANTLYGSR NVKNTIENME ELDIPILKEL
     VEHITPIREL EQAIKSCIDD HGHIMDGASS QLRSIRSSIR TLESRIREKL ENYTRSNSKM
     LSDAIITIRN DRYVLPVKQE YRGAIGGIVH DQSASGQTLF MEPKAVVDIN NSLHESKSKE
     QLEIERILKD LSNQVASYEQ DLLENVKVLT NIDFIYARGK LAQAMKASRP KMNDEGYMKM
     QQARHPMIPI DEVVANDIEF GREYTSIVIT GPNTGGKTVT LKLVGLCTLM AQSGLQVPAL
     DGCEMPVFDE VFADIGDEQS IEQNLSTFSS HMTNIVDIMK KITDRSLVLF DELGSGTDPQ
     EGAALAMAIL DEVISKQARV IATTHYPELK AYGYNREQVV NASVEFNVET LKPTYRLLIG
     VPGRSNAFDI STRLGLERAT IERAKSLIGV DSKSVENMIA SLEKSHLEAE QDYEQAHDVL
     LESEKLRNAL EHEWNLFEQK KEKLYKKAEE KAEKAIQKAR EEAETIVSEM RQMKDSAGLK
     EHEWIEARKM LDEAKPNLTK NGNQKQVDPK PVEDRQLQPG DEIKLLTVNQ MGEVLERVSD
     KEYLVQVGIM KVKVKRKDLE LIRKPKKKQV DPVTTIKGSN YHVSTELDLR GERYEDAILR
     LEKYVDDVLL AGYPKASIIH GKGTGALRKG VQEFVGRHPR IKGARPGESG EGGSGVTVIQ
     LG