ID   MUTS2_CLOBM             Reviewed;         788 AA.
AC   B1L0S3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=CLK_2516;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA56909.1; -; Genomic_DNA.
DR   RefSeq; WP_012344715.1; NC_010520.1.
DR   AlphaFoldDB; B1L0S3; -.
DR   SMR; B1L0S3; -.
DR   EnsemblBacteria; ACA56909; ACA56909; CLK_2516.
DR   KEGG; cbl:CLK_2516; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000722; 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_1000093349"
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;  88784 MW;  9A3A9F8AB8F5CAE9 CRC64;
     MKDKSIKVLE FNKIQEILKN YTCTKAAKDI IEDLKPYDSV YEVREHLEET KEAFKLLITK
     GAPPFEGVYD IRNGIYLAEK GSALLPGQLL KIAAVLRCAR RFKEYINHKE EEESYRVLEN
     ICEGIFSLPK IEEEIFNAIE GEDEIADRAS SILYNIRRSL KEKNYSVRDK INSLVRSYSS
     YLQENIYTVR GDRYVLPVKV EHKGAVPGLV HDQSSTGATL FIEPMSLVNL NNEIKELMLK
     EKAEIERILT VLSAKINANI TGVKTDANIV WELDFIFAKA KFASEYNCTC PTINDEGIVD
     IIEGRHPLID RREVVPISVK LGEEFTSLMI TGPNTGGKTV TLKTVGLIHL MAMSGLMIPA
     RENSVISYFN NVFADIGDEQ SIEQSLSTFS SHMKNIVEIM DKADENSLVL FDELGAGTDP
     TEGAALAISI LENLRKRGAK IIATTHYSEL KAYALRKEGV ENASVEFDVE TLRPTYRLLI
     GIPGKSNAFE ISKRLGLPDY IIDFARENIS NENIRFEELI QNLQEKSIKA QEDARLAENL
     KLERDKEKKK YEEKLEGLQK VRDNALIDAR REAKNIIKEA KEEADKILKD IRQLERMGYS
     SDARRKLEEE RKKLKDKLDS IEEKEIKTVH KGEALKNVKE GDEVLLASIN QKVIVLSKPD
     NKGDVLVQAG IMKITANIKD LRAAKGSNFN INSSKTKKSK KLNLNLRKVE SSVDLRGMDA
     EEAIYTVDKY LDEAYLGGLG EVTIVHGKGT GVLRKTIMDM LKGHPHVKRH RLGEYGEGGT
     GVTVVEIK