ID   MUTS2_FINM2             Reviewed;         783 AA.
AC   B0S1P2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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=FMG_0864;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
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; AP008971; BAG08282.1; -; Genomic_DNA.
DR   RefSeq; WP_012290675.1; NC_010376.1.
DR   AlphaFoldDB; B0S1P2; -.
DR   SMR; B0S1P2; -.
DR   STRING; 334413.FMG_0864; -.
DR   PRIDE; B0S1P2; -.
DR   EnsemblBacteria; BAG08282; BAG08282; FMG_0864.
DR   KEGG; fma:FMG_0864; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001319; 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..783
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093358"
FT   DOMAIN          708..783
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   783 AA;  88979 MW;  4588F28630851CA5 CRC64;
     MDKKTLNTLE YNEIKNKIEK LCKSKLGKSI ANKLEPMIEE DEIRQSLDET YEAMSMIYKF
     SNPPIYEIIN VKASIMHVSK GGYIVPEVLL KIGQILNSVH DIKRYAGESD ENYENCPMIM
     AMMDSLVEEP DLVATINNAI ISEDEISDNA SRNLARIRQT KRQKTENIRD KINSILSSND
     QALQENIVTM RDDRYVIPVK VSHKSSFKGI VHDHSSSGQT VYIEPMEVVE LNNELRMLEA
     EEREEIIRIL KEISDRVYDV KDSIFVDQDV LSKLDFIFAK AKYAIEIDAT NPKLNTNGYF
     NFKNARHPLL DKKKVVPISI YLGDDYNTLV ITGPNTGGKT VTLKTVGLIT LMAQSGILIP
     VDENSEVAIF DNIFTDIGDE QSIEQSLSTF SAHMKNIVHI VNNITFNSLV LFDELGAGTD
     PTEGAALAIA ILRIFLYKSI RTIATTHYSQ LKIFALTEKY VKNGSVEFDV NTLSPTYKLR
     IGIPGKSNAF EISRRLGLDD DIINNAKEIL SQEDKDFEDV LSDIESKKKQ IDEDKQRQLE
     LKEDLLKLRD RYEKEIEKTK LEKEKIINEA KENANEIYMR AKEESRELIN KLKFLEKESD
     ARTVANDVEN KFNKRIKKSS NKKLLNETSK KQKLQLGDEV EILGIEQQGT IVSEPDKKGD
     LLVQVGILKI NANVKNLKKI KEKEVIQSSK SIKSIIKNKA NSDIKSEIDL RGKNIEEAIY
     ELDKYIDDCV IVGLKKVNII HGKGTGMLRK GIREYLRSDK RVKKIEDAGY NEGGLGATFI
     YLK