ID   MUTS2_LACPL             Reviewed;         787 AA.
AC   Q88V16; F9UQJ0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=lp_2271;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79479.1; -; Genomic_DNA.
DR   RefSeq; WP_011101700.1; NC_004567.2.
DR   RefSeq; YP_004889993.1; NC_004567.2.
DR   AlphaFoldDB; Q88V16; -.
DR   SMR; Q88V16; -.
DR   STRING; 220668.lp_2271; -.
DR   PRIDE; Q88V16; -.
DR   DNASU; 1061270; -.
DR   EnsemblBacteria; CCC79479; CCC79479; lp_2271.
DR   KEGG; lpl:lp_2271; -.
DR   PATRIC; fig|220668.9.peg.1922; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; Q88V16; -.
DR   BioCyc; LPLA220668:G1GW0-1964-MON; -.
DR   Proteomes; UP000000432; 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   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..787
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093370"
FT   DOMAIN          712..787
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         336..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   787 AA;  87220 MW;  F059F850A3E7BC39 CRC64;
     MNSKVLNTLE YQQVKQQLAP YLVSATGQQA LNELHPMTSV ADIQRALDET NDGAEVYRLK
     GGIPVARLAD IKPHMKRLAI GATLNGSELG QVGRVLRTTR AITRFFAELL EDAPENDIRH
     LFDEVAELVT LPDVTKRLAT AIEGDGHITD EASPELSRIR SNIRRTETEI RNQMGHYTRG
     HDAKYLSDPI ITIRNDRYVI PVKAENRSRF GGIVHDQSAS GQTLFIEPQA VMAMNDRLRQ
     NQVAEKQEEQ RILEELSNLI APYQDEIINN AAILGHFDFI NAKARYAHDM KATEPAVSPQ
     NEVYLRQARH PLIDPRKVVA NDISLGTDYQ AMVITGPNTG GKTITLKTLG LLQLMAQSGL
     FIPVEAGSRV GVYNEIFADI GDEQSIEQNL STFSSHMENI ESFLAQIDAH SLVLVDELGA
     GTDPQEGAAL AIAILDAIGA KGTQVVATTH YPELKAYGFN RPDTINASME FDEETLKPTY
     RLLVGIPGRS NALDIAQRLG IPQAIVDQAR SLTDTDSQDL NAMIADLVTK RKQVEDEQLH
     LKTQVADSEK LHRQLKSEFN AYQQRKDQLI EDAKVQANTI VEQSKTKADA IISDLRKKQL
     ASGTATVKEN ELIDAKGALN ALEQQPKLKK NRVLRRAKAQ HDFHEGDDVL VKSYGQRGVL
     MRQMGKHEWE VQLGILKMKI SDGDLERVKP EEPKRARATV QSAHASHVSP NLDLRGVRYE
     DAMTQVDRYI DAALLAGYPS VTIVHGKGTG ALREGITNYL KSNRQVKSFH FAAPNHGGNG
     ATEVQFK