ID   MUTS2_CLOBJ             Reviewed;         788 AA.
AC   C1FKL4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=CLM_3528;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001581; ACO86481.1; -; Genomic_DNA.
DR   RefSeq; WP_003357786.1; NC_012563.1.
DR   AlphaFoldDB; C1FKL4; -.
DR   SMR; C1FKL4; -.
DR   STRING; 536232.CLM_3528; -.
DR   EnsemblBacteria; ACO86481; ACO86481; CLM_3528.
DR   KEGG; cby:CLM_3528; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001374; 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..788
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000192215"
FT   DOMAIN          713..788
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         332..339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   788 AA;  88648 MW;  5E33DA2ABEB806FA CRC64;
     MKDKSIKVLE FNKIQEILKN YTCTKAAKDI IEDLKPYDSM YEVREHLEET KEAFKLLITK
     GAPPFEGVYD IRSGISLAEK GSALLPGQLL KIAAVLRCAR RFKEYINHKE EEESYRVLEN
     ICEGIFSLPK IEEEIFNAIE GEDEIADRAS STLYNIRRSL KEKNYSVRDK INSLVRSYSS
     YLQENIYTVR GDRYVLPVKA EHKGAVPGLV HDQSSTGATL FIEPMSLVNL NNEIKELMLK
     EKAEIERILT VLSAKINANI TGVKTDANIV WELDFIFAKA KFASEYNCTC PTINDEGIVD
     IIEGRHPLID RREVVPISVK LGEEFTSLMI TGPNTGGKTV TLKTVGLIHL MAMSGLMIPA
     RENSVISYFN NVFADIGDEQ SIEQSLSTFS SHMKNIVEIM DKADENSLVL FDELGAGTDP
     TEGAALAISI LENLRKRGTK IIATTHYSEL KAYALRKEGV ENASVEFDVE TLRPTYRLLI
     GIPGKSNAFE ISKRLGLPDY IIDFARENIS NENIRFEELI ENLQEKSIKA EEDARLAENL
     KLERDKEKKK YEEKLEGLQK VRDNALIDAR REAKNIIKEA KEEADKILKD IRQLERMGYS
     SDARRKLEEE RKKLKDKLDS IEEKEIKTVH EGEALKNVKE GDEVLLASIN QKVIVLSKPD
     NKGDVLVQAG IMKITANIKD LRAAKGSNSN NSSSKIKKSK KLNLNLRRVE SSVDLRGMDA
     EEAIYTVDKY LDEAYLGGLG EVTIVHGKGT GVLRKTIMDM LKGHSHVKKY RLGEYGEGGT
     GVTVVELK