ID   MUTS2_CLOD6             Reviewed;         792 AA.
AC   Q189Q3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=CD630_07090;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ67542.1; -; Genomic_DNA.
DR   RefSeq; WP_011860930.1; NZ_CP010905.2.
DR   RefSeq; YP_001087185.1; NC_009089.1.
DR   AlphaFoldDB; Q189Q3; -.
DR   SMR; Q189Q3; -.
DR   STRING; 272563.CD630_07090; -.
DR   EnsemblBacteria; CAJ67542; CAJ67542; CD630_07090.
DR   KEGG; cdf:CD630_07090; -.
DR   KEGG; pdc:CDIF630_00824; -.
DR   PATRIC; fig|272563.120.peg.729; -.
DR   eggNOG; COG1193; Bacteria.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; Q189Q3; -.
DR   BioCyc; PDIF272563:G12WB-819-MON; -.
DR   Proteomes; UP000001978; 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..792
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093350"
FT   DOMAIN          717..792
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   792 AA;  88204 MW;  48496FA9C55C2D1D CRC64;
     MNEKSLRVLE YNKIIDLLKK KASSSLGLKY IENLVPNTDF VEVKSMLEET SEAQSIIIKR
     GSVGLEGIHD IEDKVKRAYI GASLDPGSLI MIADTLRVAR RLRNSLSSSD EEDFNYPIIQ
     SLSNSLYVYK DIEDQIYNAI ISEVEISDNA SSILRDIRRR IAQKNQSIRS KLNSIISSTT
     YQKYLQDAII SLRGDRFVVP VKSEYRSQVA GIVHDQSSSG ATLFIEPMTI VEMNNELRQL
     KLGEQEEIER ILSELSAMVG EVSEDLISNQ EILGRLDFAF SKGKLSIQMR GIEPTLNEDK
     YLNIKNGRHP LLDKKKVVAN TIYLGRDFHT LVITGPNTGG KTVTIKTVGL FALMTQSGLH
     IPADYGSSMC VYDNVFADIG DEQSIEQSLS TFSSHMTNIV SILQNVTADS LVIFDELGAG
     TDPVEGAALA IAVLEDINSV GAKCIATTHY SELKNYALTK SGVENAAVEF DIETLSPTYK
     LLIGVPGKSN AFEISRKLGL SDYVISRAKE YINTENIALE DVLQNVEKNR IKAVEDREEA
     ERLKEEIEKL KVEYDEKLEK LVSQRDKMIE KAKSEAFSII RQAKEEVDII IKELRSLEQE
     RASKEKNRKI EELRKELTSS MGSLQPTVKS MIVPKVSNKE IKDLKPGEEV KVITLNQNGS
     VVSVDKKRKE AVVQIGIMKM TLPFKSLQKT RKDVSTNVTK STRNIIRSKS GSVKNEVDLR
     GLNLEEAIME VEKYLDDAYV AGLESVTVIH GIGTGVLKAG LQDILRRNRH VKSQRGGQYG
     EGGAGVTIVK LK