ID   MUTS_THEYD              Reviewed;         852 AA.
AC   B5YJY3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=THEYE_A0706;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is possible that it carries out the mismatch recognition step. This
CC       protein has a weak ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00096}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000255|HAMAP-Rule:MF_00096}.
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DR   EMBL; CP001147; ACI20467.1; -; Genomic_DNA.
DR   RefSeq; WP_012545203.1; NC_011296.1.
DR   RefSeq; YP_002248548.1; NC_011296.1.
DR   AlphaFoldDB; B5YJY3; -.
DR   SMR; B5YJY3; -.
DR   STRING; 289376.THEYE_A0706; -.
DR   EnsemblBacteria; ACI20467; ACI20467; THEYE_A0706.
DR   KEGG; tye:THEYE_A0706; -.
DR   PATRIC; fig|289376.4.peg.698; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_4_0_0; -.
DR   InParanoid; B5YJY3; -.
DR   OMA; TPMMAQY; -.
DR   OrthoDB; 15991at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00096; MutS; 1.
DR   InterPro; IPR005748; DNA_mismatch_repair_MutS.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53150; SSF53150; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   TIGRFAMs; TIGR01070; mutS1; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..852
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_1000093652"
FT   BINDING         615..622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   852 AA;  97306 MW;  D3368DA92FB2B990 CRC64;
     MEVSQEELTP LMRQYLRVKE QYKDAIVFFR LGDFYEMFGE DAVIASKILG ITLTSRDKSK
     EKAIPMCGIP YFSADSYIEK LLREGYKVAI CEQIGDPKTS KGIVEREVIK VLTPGTYLPE
     GVRENIYIMS IYPSKGKIGI ALADITTGQF FLYETDKNIT DEIERFEPKE ILIPASFEDS
     LKFEISSYNK TFIEDWKFDY LLAYKTLLEH FKVASLKSYG AEEFSNAISA GGALLKYLEE
     NKQQTEFKGI KILNLSEFML LDASTKKNLE IFVSLDGSRE GSLIWVLDET LTPMGARFLK
     NTLSCPLLNI SEIEKRFDGI EAFCGDYLLR EKLEKILKDF PDIERIALKI KGKSINPKEL
     NSLKNALKRI PELREVLRNK TEILNSLYNS LYELNELVTK IENALTENPP PVITEGGIFR
     DGYNSTIDEL RALRTESKKY ILNMEAEERK KTGINSLKIG YNRVFGYYIE VTKPNLHLVP
     SHYIRKQTLA NAERFITEEL KELELKIMSA EEKLKILEQE LFIELVNSIL PFTDKILNNG
     ETIGFIDFLL SLAKVASKYN YVRPEINEED IIEIKDGRHP VIERLIQLGK LYEGRFIPND
     LLIGPADQRI IILTGPNMAG KSTYMRQNAL IVLMAQIGSF VPAKYAKIGI VDRIFTRIGA
     SDYLAKGQST FMVEMIETAN ILNNATPKSF IILDEVGRGT STFDGISIAW SVVEYIAEKI
     KARTLFATHY HELTDLAFNL DCIKNFTVVV KEWGDEIIFL RKIQEGGADK SYGIQVARLA
     GLPLEILNRA REILHRLEKK EFQVFPIRAR QLDLFFQGDP IKAELSKIDI DSLNPQKALK
     KLKELKEMLK ND