MUTS2_THEMA
ID MUTS2_THEMA Reviewed; 757 AA.
AC Q9X105;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
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}; Synonyms=mutSB;
GN OrderedLocusNames=TM_1278;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, ATPASE ACTIVITY, NUCLEASE ACTIVITY, DNA-BINDING, ACTIVITY
RP REGULATION, SUBUNIT, AND INTERACTION WITH MUTL.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=22545085; DOI=10.1371/journal.pone.0034529;
RA Jeong E., Jo H., Kim T.G., Ban C.;
RT "Characterization of multi-functional properties and conformational
RT analysis of MutS2 from Thermotoga maritima MSB8.";
RL PLoS ONE 7:E34529-E34529(2012).
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 (Probable). Has ATPase activity.
CC Binds to DNA. {ECO:0000255|HAMAP-Rule:MF_00092,
CC ECO:0000269|PubMed:22545085, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Nuclease activity is stimulated by interaction
CC with MutL and inhibited in the presence of non-hydrolytic ATP (ADPnP).
CC ATPase activity is stimulated by DNA. {ECO:0000269|PubMed:22545085}.
CC -!- SUBUNIT: Homodimer. Interacts with MutL. {ECO:0000255|HAMAP-
CC Rule:MF_00092, ECO:0000269|PubMed:22545085}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain, followed by a
CC dimerization domain and a C-terminal domain, called the small MutS-
CC related (Smr) domain, which is absent from MutS and contains the
CC endonuclease activity. {ECO:0000250}.
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; AE000512; AAD36353.1; -; Genomic_DNA.
DR PIR; B72273; B72273.
DR RefSeq; NP_229083.1; NC_000853.1.
DR RefSeq; WP_004079958.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X105; -.
DR SMR; Q9X105; -.
DR STRING; 243274.THEMA_07945; -.
DR DNASU; 898205; -.
DR EnsemblBacteria; AAD36353; AAD36353; TM_1278.
DR KEGG; tma:TM1278; -.
DR eggNOG; COG1193; Bacteria.
DR InParanoid; Q9X105; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000008183; 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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..757
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115238"
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; 86626 MW; 818F8C4F5C20426B CRC64;
MDYLESLDFP KVVEIVKKYA LSDLGRKHLD TLKPTVNPWD ELELVEELLN YFNRWGEPPI
KGLNDISQEV EKVKSGSPLE PWELLRVSVF LEGCDILKKE FEKREYSRLK ETFSRLSSFR
EFVEEVNRCI EQDGEISDRA SPRLREIRTE KKRLSSEIKR KADDFVRTHS QILQEQMYVY
RDGRYLFPVK ASMKNAVRGI VHHLSSSGAT VFLEPDEFVE LNNRVRLLEE EERLEISRIL
RQLTNILLSR LNDLERNVEL IARFDSLYAR VKFAREFNGT VVKPSSRIRL VNARHPLIPK
ERVVPINLEL PPNKRGFIIT GPNMGGKTVT VKTVGLFTAL MMSGFPLPCD EGTELKVFPK
IMADIGEEQS IEQSLSTFSS HMKKIVEIVK NADSDSLVIL DELGSGTDPV EGAALAIAII
EDLLEKGATI FVTTHLTPVK VFAMNHPLLL NASMEFDPET LSPTYRVLVG VPGGSHAFQI
AEKLGLDKRI IENARSRLSR EEMELEGLIR SLHEKISLLE EEKRKLQKER EEYMKLREKY
EEDYKKLRRM KIEEFDKELR ELNDYIRKVK KELDQAIHVA KTGSVDEMRE AVKTIEKEKK
DLEQKRIEEA TEEEIKPGDH VKMEGGTSVG KVVEVKSGTA LVDFGFLRLK VPVSKLRKTK
KEEKKETSTF SYKPSSFRTE IDIRGMTVEE AEPVVKKFID DLMMNGISKG YIIHGKGTGK
LASGVWEILR KDKRVVSFRF GTPSEGGTGV TVVEVKV
