ID   MUTS2_STACT             Reviewed;         782 AA.
AC   B9DPU2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Sca_0762;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL27672.1; -; Genomic_DNA.
DR   RefSeq; WP_015900014.1; NC_012121.1.
DR   AlphaFoldDB; B9DPU2; -.
DR   SMR; B9DPU2; -.
DR   STRING; 396513.SCA_0762; -.
DR   GeneID; 60545539; -.
DR   KEGG; sca:SCA_0762; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   BioCyc; SCAR396513:SCA_RS03860-MON; -.
DR   Proteomes; UP000000444; 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..782
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000118565"
FT   DOMAIN          707..782
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         336..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   782 AA;  88129 MW;  4C385F2CD067F005 CRC64;
     MRQKTLDVLD FDKIKAQVEN EAVSDLGRVK AAAMTPASDY ETVVFQMNET DELSQIYNKH
     RLPSLSGLTE VKPLIHRAKI GSILNVRELN QIKRLIQVQN QYKTFYSQLL EEEEAINYPI
     LDERMAQLPI LTDLYQEIHQ KCDAYDLFDD ASHELQSIRS RIHSTSQRIK QNLDRIVKSQ
     SNQKKLSDAI ITVRNDRHVI PVKAEYRQDF NGIVHDQSSS GQTLYIEPSA VVEMNNKISR
     LRNDEKVEVE RILSVLSGEV AAEADACLIA ESVMGQIDFL TAKARYGQSI KGTKPEFTEE
     RNVYLPKAFH PLLDRATVVA NTIEFAEDIQ TVIITGPNTG GKTVTLKTLG LIIVMAQSGL
     LIPALDGSKL SVFDNVYCDI GDEQSIEQSL STFSSHMKNI VEILKHADHN SLILFDELGA
     GTDPSEGAAL AMSILDHVQK LGSLVMATTH YPELKAYSYN REGVMNASVE FDVNILSPTY
     KLLMGVPGRS NAFEISSKLG LSGNIIREAK SLIGQDEQEI NNMIASLETN AKKVEDQRIE
     LDRLLREAKQ VHGDLNKKYE QYQNYEKQLM DDAKVKANQR VKAATKEADD IIKDLRHMRD
     EKNAEVKEHE LIEKRKHLDE QYEGTDIKQN VKKQKWDEIQ AGDEVKVLTY GQKGEVLEIL
     DDDEAVVQMG IIKMKLPIAD LEKKKKAQEK PAKTVSRTNR SAVKMELDLR GYRYEEAITA
     LDQYLDQAML SNYENVYIIH GKGTGALQKA VQQHLKKHKN VASFRTGMPS EGGFGVTVAE
     LK