ID   MUTS2_BREBN             Reviewed;         785 AA.
AC   C0Z9F1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
GN   OrderedLocusNames=BBR47_16440;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH42621.1; -; Genomic_DNA.
DR   RefSeq; WP_012685367.1; NC_012491.1.
DR   AlphaFoldDB; C0Z9F1; -.
DR   SMR; C0Z9F1; -.
DR   STRING; 358681.BBR47_16440; -.
DR   PRIDE; C0Z9F1; -.
DR   EnsemblBacteria; BAH42621; BAH42621; BBR47_16440.
DR   KEGG; bbe:BBR47_16440; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001877; 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..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000192214"
FT   DOMAIN          710..785
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   785 AA;  88145 MW;  C732D46141052BAE CRC64;
     MEQRVLKTLE YDKIVALLID KASCTYGKEK ASELIPFLRL DEVINAQQGT EQAATVLRLK
     GSVPLGGIRD IRGPVQRARL NAMLAPMELL DIASTVMAGR RLKTFLLDMC DDHELPLLQQ
     QAERIEGLRE LETEIRRCVD ENGDILDSAS LELRQVRQEI RQLESRIREK LDQMTRSSTY
     QKMLMENIVT IRGDRFVIPV KQEYRSVFGG IVHDQSASGA TLFIEPEVIV EMNNKLRELR
     LREEREVERI LYVLTEQVSF AVEALVENTE ALTELDFMFA KAQLAWSMKA ICPRINDRGY
     VNMRKARHPL IPREVVVPVD VELGGEYQAI VVTGPNTGGK TVSLKTIGLL SLMTMAGLHI
     PAEEESEMTV FSSIFADIGD EQSIEQSLST FSSHMTNIIQ ILAKMDDKSL VLFDELGAGT
     DPTEGAALAM SIIDHVIDSG ARLVATTHYS ELKAYAYDRP EVINASVEFD VQTLRPTYRL
     LIGVPGRSNA FAIARRLGLP EHIIDVARGS ISEEDNQVES MIASLERNRK SAEADRLAAK
     AARQEAEELR TQLEEERAQF AEEKNKRMER AEDEARIAVQ LAKEEAETII RELREMMAEG
     MEIKEHRLID AKKRLGNAVL ELEKEKVKKP AKAVRATQIK VGDEVMVTSF GQKGTVLEKV
     NNEEFLVQIG IMKMKVKRDD MHVQNSIQQK PQAAPYTSVK RRSDNIKMDL DLRGYNVEDS
     IREIDQFLDD ALLAGLHSVS IIHGHGTGVL RKGVHEYLRS HRNVKSFRLG GQGEGGVGAT
     IAELK