ID   MUTS2_THEP1             Reviewed;         757 AA.
AC   A5IMS8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Tpet_1493;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) 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; CP000702; ABQ47501.1; -; Genomic_DNA.
DR   RefSeq; WP_011943928.1; NC_009486.1.
DR   AlphaFoldDB; A5IMS8; -.
DR   SMR; A5IMS8; -.
DR   STRING; 390874.Tpet_1493; -.
DR   EnsemblBacteria; ABQ47501; ABQ47501; Tpet_1493.
DR   KEGG; tpt:Tpet_1493; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_0; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000006558; 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..757
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075480"
FT   DOMAIN          681..756
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         321..328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   757 AA;  86450 MW;  B9818D7C2D600C36 CRC64;
     MDYLESLDFP KVVEIVKKYA LSDLGRKHLD TLKPTVNPWD ELELVEELLN YFARWGEPPI
     KGLNDISQEV ERVKSGSALE PWELLRVSVF LEGCDILKKD FEKREYSRLK ETFSRLSSFR
     DFVEEVNRCI EQDGEISDRA SPRLREIRTE KKRLSSEIKR KADDFVRTHS QILQEQMYVY
     RDGRYLFPVK ASMRNAVRGI VHHLSSSGAT VFLEPDEFVE LNNRVRLLEE EERLEISRIL
     RQLTNILLSR LNDLERNVEL IARFDSLYAR VKFAREFNGT VVKPSSRIRL VNARHPLIPK
     ERVVPINLEL PPNKRGFIIT GPNMGGKTVT VKTVGLFTAL MMSGFPLPCD EGTELKVFPK
     IMADIGEEQS IEQSLSTFSS HMKKIVEIVK NADSDSLVIL DELGSGTDPV EGAALAVAII
     EDLLEKGATI FVTTHLTPVK VFAMNHPLLL NASMEFDPET LSPTYRVLVG VPGGSHAFQI
     AEKLGLDKRI IENARSRLSR EEMELEGLIR SLHEKISLLE EEKRKLQKER EEYMKLREKY
     EEDYKKLRRM KIEEFDKELR ELNDYIRKVK KELDQAIHVA KTGSVDEMRE AVKTIEKEKK
     DLEQKRIEEA TEEEIKPGDH VKMEGGTSVG KVVEVKSGTA LVDFGFLRLK VPVSKLKKAK
     KEEKEESSAV SYRPSSFRTE IDIRGMTVEE AEPVVKKFID DLMMNGISKG YIIHGKGTGK
     LASGVWEILR KDKRVVSFRF GTPSEGGTGV TVVEVKV