ID   MUTS2_STAS1             Reviewed;         782 AA.
AC   Q49WR1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=SSP1651;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18796.1; -; Genomic_DNA.
DR   RefSeq; WP_011303384.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49WR1; -.
DR   SMR; Q49WR1; -.
DR   STRING; 342451.SSP1651; -.
DR   EnsemblBacteria; BAE18796; BAE18796; SSP1651.
DR   KEGG; ssp:SSP1651; -.
DR   PATRIC; fig|342451.11.peg.1650; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000006371; 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..782
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093385"
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;  88386 MW;  379CEE5FF7213B8B CRC64;
     MRQKSLNVLE FDKIKALIEN ETISDLGKEK VVDMAPATDF NTVEFQMNET DEISQIYNKH
     RMPSLSGLAK ISTYIHRAKI GGVLSVSELN VIKRLIQIQN QYKTFYNNLL NEEETINYPI
     LNDRMEQLPV LSDLYQSIHQ KCDTYDLYDN ASYELQGIRS KISSTNQRIK QNLDKIVKSQ
     ANQKKLSDAI VTVRNERNVI PVKAEYRQDF NGIVHDQSAS GQTLYIEPSS IVEMSNQISR
     LKNDEAIERE RILSALTVEV AEEADACLIS ESIMGQIDFL TAKARYASSI KGTKPQFTKD
     RTVYLPKAFH PLLDKQTVVA NTIEFAQDIE TVIITGPNTG GKTVTLKTLG LIIVMAQSGI
     LIPTLDGSQL SIFENVYCDI GDEQSIEQSL STFSSHMKNI VEILQDTTKN SLILFDELGA
     GTDPSEGAAL AMSILDHVHE IGSLVMATTH YPELKAYSYN REGVMNASVE FDVNTLSPTY
     KLLMGVPGRS NAFDISKKLG LNMKVIQKAK SMIGQDEQEI NEMIASLESN SKRVDEQRIE
     LDYLLREAQD THDALAKQYE QYQNHEKQLM NEAKEKANQR VKSATKEADD ILKELRELRD
     QKGADVKEHE LIDKKKQLDD QYEAKSLKQN VQKKKWDEIN AGDEVKVLTY GQKGEVLELI
     DNNEAVVQMG IIKMKLPLED LEKTKKTKSE PTKMIKRENR QSIKMELDLR GYRYDEAMVA
     VDQYLDQAVL SNYEQVYIIH GKGTGALQKG VQNHLKRHKS VASYRNGMPS EGGFGVTVVE
     IK