ID   MUTS2_STRGC             Reviewed;         777 AA.
AC   A8AUW9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SGO_0260;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(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; CP000725; ABV09884.1; -; Genomic_DNA.
DR   RefSeq; WP_011999790.1; NC_009785.1.
DR   AlphaFoldDB; A8AUW9; -.
DR   SMR; A8AUW9; -.
DR   STRING; 467705.SGO_0260; -.
DR   PRIDE; A8AUW9; -.
DR   EnsemblBacteria; ABV09884; ABV09884; SGO_0260.
DR   KEGG; sgo:SGO_0260; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001131; 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..777
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093390"
FT   DOMAIN          702..777
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   777 AA;  87381 MW;  D2067C87E46809FE CRC64;
     MNTKILETLE FNKIKDLFQG SLQTEQGKLE LQVLQPTTKK EAIERAFLEV TDMEQILVED
     PHFHLAATKD ITAISKRLEL DGDLNIEELL VLKKVLRVSH DLVTFYNDLE NVRLQELNRI
     FENLVDFPAI QGSLLAVNDG GFIESFASEE LGRIRRKIQE NESKVRDLLQ EILKNKGDML
     ADQVVASRNG RNVLPVKNTY RNRIPGVVHD ISASGTTIYI EPRAVVNLNE EISNYKADER
     YELLRILQEL SAMIRPHAAE IANNAWIIGH LDLVMAKLAF MRERGAVVPA ISDTQAIQLL
     QVRHPLIQNA VANDLHFGPD LTEIVITGPN TGGKTIMLKT LGLAQIMAQS GLPILADKGS
     RVGIFSQIFA DIGDEQSIEQ SLSTFSSHMT NIVSILEQVD SESLVLLDEL GAGTDPQEGA
     ALAIAILEDL RLRQIKTMAT THYPELKAYG IETDWVENAS MEFDTDSLRP TYRFMQGVPG
     RSNAFEIARR LGLSEVIVSH AQEQTNTDSD VNQIIERLEE QTLESRKRLD NIREVEQENL
     KFNRALKKLY NEFNREKETE LNKARLEAQE IVDLALSESE SILKNLHAKS SLKPHEIIEA
     KAQLKKLAPE TVDLSKNKVL KQAKKNRAPK VGDDILVTSY GQRGTLVKLL KDGRWEAQVG
     LIKMTLEEQE FNLLKAEKEQ QPKRKQVNVV KRANTAGPRA RLDLRGKRYE EAMKELDEFI
     DQALLNNMAQ VDIIHGIGTG VIREGVNKYL RRNKHVKSFG YAPQNAGGSG ATIVIFK