ID   MUTS2_STRA3             Reviewed;         779 AA.
AC   Q8E3J5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-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=gbs1764;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
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; AL766853; CAD47423.1; -; Genomic_DNA.
DR   RefSeq; WP_001060328.1; NC_004368.1.
DR   AlphaFoldDB; Q8E3J5; -.
DR   SMR; Q8E3J5; -.
DR   STRING; 211110.gbs1764; -.
DR   EnsemblBacteria; CAD47423; CAD47423; CAD47423.
DR   KEGG; san:gbs1764; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000823; 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..779
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093387"
FT   DOMAIN          704..779
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         328..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   779 AA;  87783 MW;  E1C4AFEC8E427C9D CRC64;
     MNNKILEQLE FNKVKELILP YLKTEQSQEE LSELEPMTEA PKIEKSFNEI SDMEQIFVEH
     HSFGIVSLSS ISESLKRLEL SADLNIQELL VIKKVLQSSS DMIHFYSDLD NVSFQSLDRL
     FENLEQFPNL QGSFQAINDG GFLEHFASPE LERIRRQLTN SERRVRQILQ DMLKEKAELL
     SENLIASRSG RSVLPVKNTY RNRISGVVHD ISSSGSTVYI EPRAVVTLNE EITQLRADER
     HEESRILHAF SDLLRPHVAT IRNNAWILGH LDFVRAKYLF MSDNKATIPE ISNDSTLALI
     NVRHPLLSNP VANDLHFDQD LTAIVITGPN TGGKTIMLKT LGLAQLMGQS GLPVLADKGS
     KIAVFNNIFA DIGDEQSIEQ SLSTFSSHMT HIVSILNEAD HNSLVLFDEL GAGTDPQEGA
     SLAMAILEHL RLSNIKTMAT THYPELKAYG IETNFVENAS MEFDAETLSP TYRFMQGVPG
     RSNAFEIASR LGLAPFIVKQ AKQMTDSDSD VNRIIEQLEA QTLETRRRLD HIKEIEQENL
     KFNRAVKKLY NEFSHERDKE LEKIYQEAQE IVDMALNESD TILKKLNDKS QLKPHEIIDA
     KAQIKKLAPQ VDLSKNKVLN KAKKIKAARA PRIGDDIIVT SYGQRGTLTS QLKDGRWEAQ
     VGIIKMTLTQ DEFTLVRVQE EQKVKSKQIN VVKKADSSGP RARLDLRGKR YEEAMQELDN
     FIDQALLNNM GQVDIIHGIG TGVIREGVTK YLRRNKHVKH FAYAPQNAGG SGATIVTLG