ID   MUTS2_SULSY             Reviewed;         763 AA.
AC   B2V693;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SYO3AOP1_1568;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD67166.1; -; Genomic_DNA.
DR   RefSeq; WP_012460222.1; NC_010730.1.
DR   AlphaFoldDB; B2V693; -.
DR   SMR; B2V693; -.
DR   STRING; 436114.SYO3AOP1_1568; -.
DR   EnsemblBacteria; ACD67166; ACD67166; SYO3AOP1_1568.
DR   KEGG; sul:SYO3AOP1_1568; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_0; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
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   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; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding.
FT   CHAIN           1..763
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093408"
FT   DOMAIN          687..762
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         330..337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   763 AA;  88008 MW;  AFCB58AD4EC85295 CRC64;
     MRERDLESLE YRKFLNLLSS YTHNEITKNK INNLKPITNR EFLEREIAKA SEFESIFLKE
     GYFPLSEFPD ITQAINLAKV EDSILSPKEI FEIGEILRVV KNVKSFLSNH TLNHLKKLFQ
     NLTPLRELEK FITDSIDSDF AVKDSASKDL ARIRKEIKEV EKLINNQLEK ILNNPNYQDA
     IQEKLITLRR DRFVIPVKYN FSHRIKGIIQ DRSSSGNTVY VEPFEVVPLN NKLTDLKLQE
     NLEIRKILRF LTDIIRTKIN FISNSFDALI EFDILYTKAK FSKAFNCRFP QIGESYQLYN
     AKHPIFLLKE KPFIPIDILL DEKRGLVITG PNTGGKTVAL KTAGLLSLIF QSAIAIPVDE
     GSKIPIFNGI FIDIGDYQSI EENLSTYSAH IKNIREMLDL ANKNSLLLFD ELIPGTDPDF
     ASAIGIAILD YVKEKNIRVI ATTHLKKIKA YVLNNDYFKI AAVGFDKETL TPTYKIYYNA
     VGESMAFYIA QKLNLQKEII EKAKSLISKD LLNFEELASK FSALISEYEE KIKEINQLKQ
     QLELEKAKYE NLAKQLEKDK KEKWKESLKE IQDFVEKIRQ EGYEVLKEVK ERQSGAPLEK
     FVKEKKNINI KTEEEIKAEE IKEGDVVRIK GKTQEGTVIA IREDKANVNF GGIKIWLPLN
     QLEKRQPKEE KTTFKITKSK TDITPSINLI GKTKEEAIKE LEKYIDKVIL EGYTTFKIIH
     GYGAGVLRNA VREYLDKLPF KLKYEDAPYH EGGLGVTIVR FEE