ID   MUTS2_GEOTN             Reviewed;         784 AA.
AC   A4IRL1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=GTNG_2620;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO67965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4IRL1; -.
DR   SMR; A4IRL1; -.
DR   STRING; 420246.GTNG_2620; -.
DR   EnsemblBacteria; ABO67965; ABO67965; GTNG_2620.
DR   KEGG; gtn:GTNG_2620; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001578; 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.
FT   CHAIN           1..784
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075477"
FT   DOMAIN          709..784
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          527..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  86843 MW;  9866B80D697F7B7E CRC64;
     MQQKMLRILE FDKVKEQLAE HASSALGLEK IAALVPSSDL DEVAVWLEET DEAAAVLRLR
     GYVPLDGVVD IRSHLKRAAI GGVLSPIELL EVAATAAASR QMKQLIMSLH DEHGGLARLA
     DYADELAEVP ALEEDIRRSI DDHGEVLDTA SDRLRSLRGQ IRAAEARIRE KLESIIRSPS
     AQKRLSDAII TIRNDRYVIP VKQEYRSAYG GIVHDQSASG ATLFIEPQVV VELNNALREA
     RAKEKQEIER ILRELSAKVA EHDEPLKRAV EALAHFDFLF AKAKYARRLQ AAKPAVNNRG
     YLRFLQARHP LIDQDKAVPN DIVLGGDYTT IVITGPNTGG KTVTLKTVGL LTIMAQAGLF
     IPAADGSEAA VFRSVFADIG DEQSIEQSLS TFSSHMVNIV DILRHVDEES LVLFDELGAG
     TDPQEGAALA IAILDEVHGR GARTVATTHY PELKAYGYNR PGVVNASVEF DTETLRPTYK
     LLIGIPGRSN AFDISRRLGL DERIIERAKV QVSAESHSVE NMIASLERSK KQAEEDEARA
     HSAREEAERL RAEWEQKLEE LEDKKAEQLA EAAQKATDII RAAEREAERI INELRRLQKE
     KQAEVKEHEL IAAKQRLAAA VPVVEKRKKT KKATARHAFQ SGDEVKVTSL NQKGYLLEKV
     SEDEWQVQLG ILKMKIHERD LEYIGSAPAK EVTPIATVKG KDAHVSLELD LRGERYEDAL
     VRLEKYIDDA VLAGYPRVSI IHGKGTGALR QGVQQFLKQH RAVKSFRFGA ANEGGTGVTV
     VELK