ID   MUTS_CALBD              Reviewed;         863 AA.
AC   B9MJU0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=Athe_1500;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) 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; CP001393; ACM60598.1; -; Genomic_DNA.
DR   RefSeq; WP_015907954.1; NC_012034.1.
DR   AlphaFoldDB; B9MJU0; -.
DR   SMR; B9MJU0; -.
DR   STRING; 521460.Athe_1500; -.
DR   EnsemblBacteria; ACM60598; ACM60598; Athe_1500.
DR   GeneID; 31772845; -.
DR   KEGG; ate:Athe_1500; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_4_0_9; -.
DR   OMA; TPMMAQY; -.
DR   OrthoDB; 15991at2; -.
DR   Proteomes; UP000007723; Chromosome.
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:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..863
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_1000192192"
FT   BINDING         607..614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   863 AA;  99295 MW;  23FCE60B41E31AB3 CRC64;
     MQELTPMMQQ YMEIKQKVKD CILFFRLGDF YEMFFEDAIV ASKELEIALT SRDCGNNEKA
     PMCGVPYHSA TSYIAKLIEK GYKVAICEQV EDPKLAKGIV KREITRIITP GTFIDDNIST
     ANNFICCISK DRSEFALTFV DVSTGEMYSC LLEEDLQKLV NEIGKYSPSE ILISNIEDEL
     YEFLKKNCTS FVQMIEFVDL QKCHEIIENQ INVGKIDEKL ILSVGNLLKY LTETQKISFD
     YIRRFEFYRV QNYLQIDINT KRNLELTESI IQRSRKNSLL GILDQTKTSM GSRLLKKWIE
     RPLIDIIEIN KRLDSVEELK SNYSTLVQVE ELLSRMYDIE RLSSKFAYKN VNAKDLLSLK
     KSIEVLPTLK QFLSSFDSEL LKEIYEGLDT LEDIYALIDS SINEDAPVSL KEGGIIKEGF
     NEEVDRLRNI SKNSKELLVE YEEKERNLTG IKNLRIGYNK VFGYYIEVTK SNYSLVPDRY
     IRKQTLANAE RYITEELKKL EDEILGADQK LIELEYQLFC EIRDRIEAQI ERIQKTASNI
     ANLDVLCSFA RIAIDNEYVR PNVYLGDRIY IKNGRHPVVE KMIGRGNFIP NDTELDQAEN
     RVLIITGPNM AGKSTYMRQV ALIVIMAQMG CFVPADEAHI GVVDKIFSRI GASDDISSGQ
     STFMVEMSEV ANILKNATPK SLIIFDEVGR GTSTYDGLSI AWAVLEYVAD KSKIGAKTLF
     ATHYHELTEL EERIPGVKNY RVDVKEEGKN IIFLRKIVRG GCDSSYGIHV ARLAGIPEEV
     LKRAEEILKQ LEEADINRKN IRKLRREIKK EFTEQIDFFS YKKEEIIDKI EKLDILNITP
     IQALNILSEL KHEIIKAKER QLI