ID   MUTS2_STRSY             Reviewed;         778 AA.
AC   A4VSW4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SSU05_0235;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(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; CP000407; ABP89203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VSW4; -.
DR   SMR; A4VSW4; -.
DR   STRING; 391295.SSU05_0235; -.
DR   EnsemblBacteria; ABP89203; ABP89203; SSU05_0235.
DR   KEGG; ssu:SSU05_0235; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000243; 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..778
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093404"
FT   DOMAIN          703..778
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         329..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   778 AA;  87678 MW;  236A93F0BCD7AC68 CRC64;
     MNNKIIETLE FHKVRQKIEP YLLTEQGFEE LRQLEPMVEV HRIQQAFDEL TDIAQIFVEN
     PYFSLAATSD IGPAMRRLEL DTDLNIAELL AVKKVLEVSK SLLDFYGNLE NVSLSQQLDK
     LFEKIELFPH LQGSLQSIND AGFVEDFASE KLARIRRKIR EAEDQVRQVM QDILKTKGDM
     LSDSILASRN GRNVLPVKNT YRNKIAGVVH DISASGSTVY IEPRAVVTLN EEISHLRAEE
     RHELNRILQE LSDMLRPHGG VIRNNAWLIG HIDFVRAKHL FARDHQAVVP KLSEKQDIAL
     LNVRHPLIAK PVPNDLYFGS QLTAIVITGP NTGGKTIMLK TLGLTHLMAQ SGLPILADKG
     SRVAIFKEIF ADIGDEQSIE QSLSTFSSHM THTVEILRAA DQDSLILFDE LGAGTDPQEG
     ASLAMAILDD LRLRGIKTMA TTHYPELKAY GIETSGIENA SMEFDSNSLR PTYKFMQGVP
     GRSNAFEIAR RLGLSDIIIQ SAQSWTDTDS DVNRIIEKLE SQTVESRQRL DKIRDVEQEN
     YKMNRALRKL YDELNREREN ELNKARLEAK EIVDMALAES EDILKNLHAA ASLKPHQIIE
     AKAELKKLAP EVVDLSKNKV LKKAKIKREA KVGDDIIVTA YGQRGTLTNQ LKDGRWEAQV
     GLIKMTLAKD EFELVKAEKA EQPKKRQVHT VKRANVRGPK ARLDLRGKRY EEAMMELDEF
     IDQALLNNLA QVDIVHGIGT GVIREGVTKY LRRNKQIKEF GYAPQNAGGS GCTIVTFK