ID   MUTS2_LACLM             Reviewed;         776 AA.
AC   A2RJC8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=llmg_0778;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(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; AM406671; CAL97380.1; -; Genomic_DNA.
DR   RefSeq; WP_011834759.1; NZ_WJVF01000008.1.
DR   AlphaFoldDB; A2RJC8; -.
DR   SMR; A2RJC8; -.
DR   STRING; 416870.llmg_0778; -.
DR   EnsemblBacteria; CAL97380; CAL97380; llmg_0778.
DR   KEGG; llm:llmg_0778; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; A2RJC8; -.
DR   BioCyc; LLAC416870:LLMG_RS04015-MON; -.
DR   Proteomes; UP000000364; 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..776
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093368"
FT   DOMAIN          701..776
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         330..337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   776 AA;  87377 MW;  89CD1D3EE006E2C2 CRC64;
     MNKKILQILE YDKVKEQFMN ALTTAQGQKE LSDLVPLTDK DKIQLLFDEV ADFRLLTQEN
     GLLNLGKTND LTEILRRLEL EASLSGKEFV EIKKVIQLGI NIQRFFDEAE NVETPSLNIT
     LEKLVDLSGL IKKLEIFDNA GSLYDNASLE LMHIRASIKS HQSEIRKIMQ EMLTKNLSSL
     SENVITIRND RQVLPVKAEN KNKIAGVVHD MSASGQTLYI EPNAVVSLNN KLNQKRIEER
     QEITRIYREL AEELKPYSFD IRQNAWLIGH IDFVRAKYLY LTANKASLPA LTNDKDIILF
     AARHPLIDAK MVVANDIKFD KTLNTIVITG PNTGGKTITL KTVGLLTILA QSGLPILAED
     GSRIHLFDDI FADIGDEQSI EQSLSTFSSH MTNIVQILAQ ADENSLVLFD ELGAGTDPKE
     GAALAIAILE NLRKRNVKTM ASTHYPELKA YGVETQQVIN ASMEFNIDKM QPTYHLQLGV
     PGRSNALEIS RRLGLPETII SEAGQQISES EHDVNQMIEK LEEKTREVIE SSRNIKKIER
     ENQSLHKDLT KVYNQINRER DFELEKAQKE AQEVVKKASL EAQEILKNLN DKAALKPHEI
     IAARKELEGL APTIDFSKNK VLKKAKAQRG LKQGAEVNVT SYGQRGKLIR LEKDGRWTVQ
     MGSITTRLSE EEFEVIETPE QIQAKTKNVS KKVTSKVKAQ LDLRGMRYEE AELELDNYID
     QALLANLIQI TIVHGIGTGV IREMVQKKLQ KHRHIKSYEY APINAGGSGA TIAILK