ID   MUTS2_PELTS             Reviewed;         785 AA.
AC   A5D0W6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=PTH_1939;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF60120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D0W6; -.
DR   SMR; A5D0W6; -.
DR   STRING; 370438.PTH_1939; -.
DR   PRIDE; A5D0W6; -.
DR   EnsemblBacteria; BAF60120; BAF60120; PTH_1939.
DR   KEGG; pth:PTH_1939; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000006556; 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..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093376"
FT   DOMAIN          710..785
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   785 AA;  86175 MW;  4A13ABEE807BDBC9 CRC64;
     MDKKALKRLE YHKVLEQLAA CSGSSLGREK IMAMEPLDNL QAILRKQEET SEGRKLLRLE
     PFAEAGGWKD IRAQLRKAGQ GAILDPEELL AVADTLTAGR TIRKFFQDRQ EQYPLLYEVS
     SALVSLPELE RKIKNAILPG GEVADGASPE LAQIRRRLAA AQAQVKEHLE HIIRSPSYQK
     YLQEPIVTIR EGRYVVPVKI EHRSQVPGIV HDQSASGATL FIEPMAVVEK NNELRRLMAA
     EKREIQRILA ELSAGVAQHA GPIGASLEAL GELDFIMARA RYSQKLDAWA PLLEGEACMD
     IRRGRHPLLQ GEVVPIDIRL GADFDTLVIT GPNTGGKTVA LKTAGLLVLM AQSGLHIPAG
     EGSRLGIFRQ VFADIGDEQS IEQSLSTFSS HMNNIVEIIG KAGPDSLVLL DELGAGTDPA
     EGAALAQSIL EKLHSAGAKT VATTHYGELK DFALTRERVE NASVEFDAIT LRPTYRLLIG
     KPGRSNAFEI AARLGLPEEV VKRARSFLTA EHIQAEELMR SLEKTQQEAE AERRRAAELA
     SEARALKERY EKIEADLASK RESILSKAAE EAQALVRAAR LEAEAAVREL REKMAEEAAR
     ERENAIREAR EKLRKLQQRV GRAVPEKTVP GEAPAGLRPG EEVFLTRYNQ KGYVLEPPGA
     GGEVLVQVGV IKMNVPLREL RRVKEARPAG GQSEVAGVLL NKAREISPEL DLRGLYADEA
     LLEVEKYLDD AYLAGLSRVY LIHGKGTGSL RAAIHRQLSG HRRVKSFRLG EHGEGGLGVT
     VVELA