ID   MUTS2_LEUCK             Reviewed;         801 AA.
AC   B1MXB4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=LCK_00333;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(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; DQ489736; ACA82166.1; -; Genomic_DNA.
DR   RefSeq; WP_004907415.1; NC_010471.1.
DR   AlphaFoldDB; B1MXB4; -.
DR   SMR; B1MXB4; -.
DR   STRING; 349519.LCK_00333; -.
DR   EnsemblBacteria; ACA82166; ACA82166; LCK_00333.
DR   KEGG; lci:LCK_00333; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000002166; 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.
FT   CHAIN           1..801
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093373"
FT   DOMAIN          726..801
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          696..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         336..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   801 AA;  87760 MW;  A0FECE5D048C8FA8 CRC64;
     MNNKVLQTLE YDKIKLQLND FLSTPTGLQE ANELQPVSDV DLINHWLAET ADAVLIDRLK
     GGIPLSKLSD ITPHLKRLNI EASLSATELS EMSLVLRNTS TIASFFEQMQ DEAIGESLRV
     LPEQAKNLVT LPDITRQIQI AIDSSGRLND EASYELKHVR DRINGTEQAV KNQMQAYTRG
     KTAQYLSDPI VTIRSDRYVL PVKAEYRSQF GGVVHDQSQT GQTLYVEPQA VVTLNNKLSE
     LRVQEQAEEQ RVLQELSATL APHTEEIANN VTILGHFDFV NAKARLAARL DAMQPMVNTE
     NKVDLQQAWH PLLDKDLAVA NDIALGDGYK AIIITGPNTG GKTITIKTLG ILQLMAQSGL
     FITTKRPSTV GVFHEIFADI GDEQSIEQSL STFSSHMANI VSMIDRIDDK TLVIFDELGA
     GTDPAEGAAL AIAILDKVAS LGAFVIATTH YPELKLYGYN RPETLNASMV FDVSTLKPTY
     QFLMGVPGQS NALAIAKRLG FGDDVIGAAT ALTSDADQDL NQMIADLVAQ RDAVKQHDVA
     LSEQLKATEK QSEALSEQQR QLEKERAKIV LDAKNEANHI VAATKKQAEQ MISEIRKARL
     NAGQSAGELS EQDLQAKKRQ LDGLRQNSSL EKNKILQKAK RAKQLAAGDE ITVQSYGQQG
     TLIKQHSNGQ WEVEMGILKM LVDEDDIVKT EATAKAQQSK AKQKQQKIVK TKTASGSARA
     TAKSRLDLRG VRYEAALAEL DRYLDTAVLA NLGTVEIIHG KGTGALRQGV TEFLRSDRRV
     KAYHFANANA GGDGATIAEL S