ID   MUTS2_LACLA             Reviewed;         776 AA.
AC   Q9CF36;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=LL1645;
GN   ORFNames=L0293;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05743.1; -; Genomic_DNA.
DR   PIR; E86830; E86830.
DR   RefSeq; NP_267801.1; NC_002662.1.
DR   RefSeq; WP_003129443.1; NC_002662.1.
DR   AlphaFoldDB; Q9CF36; -.
DR   SMR; Q9CF36; -.
DR   STRING; 272623.L0293; -.
DR   PaxDb; Q9CF36; -.
DR   EnsemblBacteria; AAK05743; AAK05743; L0293.
DR   KEGG; lla:L0293; -.
DR   PATRIC; fig|272623.7.peg.1767; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000002196; 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..776
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093367"
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;  87296 MW;  69061B3A64530702 CRC64;
     MNKKILQILE YDKVKEQFMN ALTTAQGQQE LKDLKPLTDK EKIQLLFDEV ADFRLLTQEN
     GLLNLGKTND LTEILRRLEL EASLSGKEFV EIKKVIQLGI NIQRFFDEAE NVETPSLAIT
     LEKLVDLSAL VKKLEIFDNA GSLYDNASLE LMHIRASIKS HQSEIRKIMQ EMLTKNLSSL
     SENVITIRND RQVLPVKAEN KNKIAGVVHD MSASGQTLYI EPNAVVSLNN KLNQKRIEER
     QEITRIYREL ASQLKPYSFD IRQNAWLIGH IDFVRAKYLY LAANKATLPE LTTDKDITLF
     AARHPLIEAK IVVTNDIKFD AGLNTIVITG PNTGGKTITL KTVGLLTILA QSGLPILAAD
     GSRIHLFDDI FADIGDEQSI EQSLSTFSSH MTNIVHILAQ ADENSLVLFD ELGAGTDPKE
     GAALAIAILE NLRERNVKTM ASTHYPELKA YGVETQRVIN ASMEFNIDKM QPTYHLQLGV
     PGRSNALEIS RRLGLPETII SVASQQISDS EHDVNQMIEK LEEKTREVIE SSRNIKKIER
     ENQSLHKDLT KVYNQINRER EFELEKAQKE AQEVVKKASL EAQEILKNLN DKAALKPHEI
     IAARKELEGL APTIDFSKNK VLKKAKAQRG LKQGAEVNVT SYGQRGKLIR LEKDGRWTVQ
     MGSITTRLNE DEFEVIESPE QIQAKTKNVS KKVTSKVKAQ LDLRGMRYEE AELELDNYID
     QALLANLIQI TIVHGIGTGV IREMVQKKLQ KHRHIKSYEY APINAGGSGA TIAILK