ID   MUTS2_GEOKA             Reviewed;         784 AA.
AC   Q5KWF8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=GK2693;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KWF8; -.
DR   SMR; Q5KWF8; -.
DR   STRING; 235909.GK2693; -.
DR   EnsemblBacteria; BAD76978; BAD76978; GK2693.
DR   KEGG; gka:GK2693; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001172; 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..784
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075476"
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;  86829 MW;  924888806B39F544 CRC64;
     MQPKVLHTLE FDKVKEQLAE HASSPLGLEK IDALMPSSDL EEVAAWLDET DEAAAVLRLA
     GYVPLDGVVD IRPHLKRAAI GGTLSPQELL EVAATSAASR QMKRLIAGLY DEHGGLERLF
     RYADTLAEAP ELEHDVRRSI DDHGEVLDAA SDRLRSLRGQ IRSVEARIRE KLESIIRSPS
     AQKRLSDAII TIRNDRYVIP VKQEYRGAYG GIVHDQSASG ATLFIEPQAV VELNNALREA
     RAKEKQEIER ILRELSAKVA EQAEPLARTV EALAALDFAF AKAKYARRLQ AAKPAVNSRG
     YLRFLQARHP LLDQEKAVPN DIELGGDYTT IVITGPNTGG KTVTLKTIGL LTLMAQAGLF
     IPAADGSEAA VFRSVFADIG DEQSIEQSLS TFSSHMVNIV DILRHVDGES LVLFDELGAG
     TDPQEGAALA IAILDEVHGR GARTVATTHY PELKAYGYNR PGVVNASVEF DTETLRPTYK
     LLIGIPGRSN AFDISRRLGL DERIIERAKA QVSAESHNVE NMIASLERSK KQAEEDEARA
     RAALEEAERL RAEWEQKWEE LEEEKAERLA EATQKAADII RAAEREAERI IQELRRLQKE
     KQAEVKEHEL VEAKQRLAAA MPKVEKRKKA KKAASRHVFQ PGDEVKVTSL NQKGYLIEKV
     SDDEWQVQLG ILKMKIHERD LEYIGSAPAK DVTPIATVKG KDAHVSLELD LRGERYEDAL
     IRLEKYLDDA VLAGYARVSI IHGKGTGALR QGVQQFLKQH RAVKSFRFGE ANEGGTGVTI
     VELK