ID   MUTS2_STAHJ             Reviewed;         783 AA.
AC   Q4L5E9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=SH1817;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05126.1; -; Genomic_DNA.
DR   RefSeq; WP_011276094.1; NC_007168.1.
DR   AlphaFoldDB; Q4L5E9; -.
DR   SMR; Q4L5E9; -.
DR   STRING; 279808.SH1817; -.
DR   PRIDE; Q4L5E9; -.
DR   EnsemblBacteria; BAE05126; BAE05126; SH1817.
DR   KEGG; sha:SH1817; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000543; 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..783
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115236"
FT   DOMAIN          708..783
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         337..344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   783 AA;  88577 MW;  C5EB1BD5736EB035 CRC64;
     MRQKTLDVLE FDKIKSFVAS ETISDLGREK VSKMSPATDF ETVEFQMNET DEISQIYNKH
     RLPSLSGLAK ISPLIHRANI GGVLNVTELN LVKRLIQVQN QFKTFYNQLL EEDEQVVKYP
     ILNDKMNQLP ILSDLFQEIN EKCDTHDLYD SASYELQGIR SKISSTNQRI RQNLDRIVKS
     QANQKKLSDA IITVRNDRNV IPVKAEYRQD FKGIVHDQSA SGQTLYIEPS SIVEMNNQIS
     RLRNDEAVER ERILTELTGM VAAEADGCLI AESVMGQIDF LTAKARYARS IKGTKPTFYK
     DRTVYLPNAY HPLLNKDTVV ANTIEFVDDI ETVIITGPNT GGKTVTLKTL GLIIIMAQSG
     LLIPTLDGSQ LSVFENVYCD IGDEQSIEQS LSTFSSHMKN IVEILQETDK NSLVLFDELG
     AGTDPSEGAA LAMSILDHVR EIGSLVMATT HYPELKAYSY NREGVMNASV EFDVNTLSPT
     YKLLMGVPGR SNAFDISRKL GLSLGIINKA KTMIGTDEQE INSMIESLEK NSKRVDEQRI
     ELDRLLKEAR KTHDDLEHQY EQYKSYEKKL MDEAKEKANQ RVKSATKEAD SILKELRTLR
     DQKGADVKEH ELIDKKKQLD DQYEAKSLKQ NVQKQKYDEI HAGDEVKVLS YGQKGEVLEL
     VSEEEAVVQM GIIKMKLPIE DLEKTKKKKE KPSKMVTRQN RQTIKTELHL RGYRYEEAVS
     ELDQYIDQAV LSNYEQVYII HGKGTGALQK AVQNHLNKHK SVKSYRGGMP SEGGFGVTVA
     ELK