ID   MUTS2_LIGS1             Reviewed;         786 AA.
AC   Q1WT38;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=LSL_1105;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99913.1; -; Genomic_DNA.
DR   RefSeq; WP_003700526.1; NC_007929.1.
DR   RefSeq; YP_535996.1; NC_007929.1.
DR   AlphaFoldDB; Q1WT38; -.
DR   SMR; Q1WT38; -.
DR   STRING; 362948.LSL_1105; -.
DR   PRIDE; Q1WT38; -.
DR   EnsemblBacteria; ABD99913; ABD99913; LSL_1105.
DR   GeneID; 57059531; -.
DR   KEGG; lsl:LSL_1105; -.
DR   PATRIC; fig|362948.14.peg.1177; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000006559; 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..786
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093371"
FT   DOMAIN          711..786
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   786 AA;  88057 MW;  68E37E23BA97C1A3 CRC64;
     MNKKVLKTLE YDKVKQNLYA FTTTSMGKRL IDKLEPSSDY DEISNSLAQT KDGADILRIK
     GGIPVPNLIS IKSFLKRLDI GGTLNSKELA AIGRVLRATN EVNRFFKDLA DNKIKLEVLF
     DDVAKLESLP EISKKLLVSI ENDGHVTDDA STLLKSIRQQ ISVTEETIRE RLNAYTRGTN
     SKYLSNAVVT IRNERYVLPV KQEYRSKFGG IVHDQSSSGQ TLFVEPAVIV ELNNRLRQQQ
     VAEREEINRI LEELSKELAP YTHELNNNAK ILGMLDFINA KAKYAHSIKA TEPILSKEND
     VYLRQVWHPL LDMKKAVKND IMIGKDYQAI VITGPNTGGK TITLKTLGLV QLMGQSGLYI
     PAFEESRIGI FDDIFADIGD EQSIEQSLST FSSHMTNIVE ILKGIDEKSL VLFDELGAGT
     DPQEGAALAI SILDAVGAKG SYVVATTHYP ELKAYGFERP NTINASMEFD ANTLQPTYRL
     LIGIPGRSNA FDISQRLGLD KMIVMAARQL TSQDSQDLNE MISDLVAKRH DAEEKEIMYR
     KYLREAEELH HDLETNFHQF ERQKENMLEQ AKERANQIVE ETKKKSDELI SELRKMKMSA
     ASNIEEGSLI DAQGRVNALH QETNLKKNKV LRKAKQQQEL HPNDDVMVNS YGQRGVLLRK
     AGNHAWEVQL GILKMKIDES DLEKIKVKDT QPKRAGAVLK SSSSSHVSPT LDLRGERYEN
     AMVKVDRYID AAVLAGYNSV TIIHGKGTGA LRTGIINYLK QNKAVKNFEF ASPNNGGNGA
     TVVYFK