ID   MUTS2_GEOSW             Reviewed;         784 AA.
AC   C5D5Q8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=GWCH70_2632;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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; CP001638; ACS25326.1; -; Genomic_DNA.
DR   RefSeq; WP_015864737.1; NC_012793.1.
DR   AlphaFoldDB; C5D5Q8; -.
DR   SMR; C5D5Q8; -.
DR   STRING; 471223.GWCH70_2632; -.
DR   PRIDE; C5D5Q8; -.
DR   EnsemblBacteria; ACS25326; ACS25326; GWCH70_2632.
DR   KEGG; gwc:GWCH70_2632; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
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..784
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000202682"
FT   DOMAIN          709..784
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   784 AA;  88538 MW;  1591E98610B9C536 CRC64;
     MHTRVLHVLE FDKVKEQLLE HVSSSLGKEK VEKLFPSSHF AEVTNWQEET DEAVAALRLR
     GHVPLGGIFD IRASLKRAKI GGTLSPHELL DIASTISASR QLKQFIESLH EEKEEFPHLA
     GYAEKLAALP EVQQAIERCI DDHGEVMDHA SERLRSIRQQ LRTTEARVRE KLENIIRSQS
     AQKMLSDAII TIRNDRYVIP VKQEYRGVYG GIVHDQSASG ATLFIEPQAV VELNNQLQEA
     RVKEKREIER ILTELTSIVA EHAEALLENV DILAQLDFIF AKAKYANKLK ATKPVMNDRG
     YIRLLQARHP LIDQDVVVPN DIELGKDYTT IVITGPNTGG KTVTLKTIGL LTLMAQAGLF
     IPALDGSELA VFRSVYADIG DEQSIEQSLS TFSSHMVNIV DILRNVDHES LVLFDELGAG
     TDPQEGAALA IAILDEVHGR GARTVATTHY PELKAYGYNR DGVINASVEF DTETLRPTYK
     LLIGIPGRSN AFEISKRLGL DERIIERAKS HISAESNKVE NMIASLEQSK KRAEEEEKKA
     KEARMEAEKL RSDWEQKWEE LHEKRDEIIE EAKRKAADIV RASQQEAERI IRELRRMQKE
     KQAEIKEHEL IEAKKRLEEA IPTLEKKKKE RKKQTQHAFQ PGDEVKVTSL NQKGYLVEKV
     SDDEWQVQLG ILKMKINERD LEYIGSAPKT ETKPLATVKG KDYHVGLELD LRGERYEDAI
     VRLEKYIDDA LLAGYPRVSI IHGKGTGALR KGVQEFLKKH RSVKNFHFGE ANEGGTGVTI
     VELK