ID   MUTS_DESRM              Reviewed;         868 AA.
AC   A4J5Q6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=Dred_1887;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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; CP000612; ABO50409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4J5Q6; -.
DR   SMR; A4J5Q6; -.
DR   STRING; 349161.Dred_1887; -.
DR   PRIDE; A4J5Q6; -.
DR   EnsemblBacteria; ABO50409; ABO50409; Dred_1887.
DR   KEGG; drm:Dred_1887; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_1_3_9; -.
DR   OMA; TPMMAQY; -.
DR   Proteomes; UP000001556; 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;
KW   Reference proteome.
FT   CHAIN           1..868
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_0000335148"
FT   BINDING         620..627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   868 AA;  97106 MW;  7E7D651DAC13EDC5 CRC64;
     MALTPMMQQY LDIKKQHPNT ILFFRLGDFY EMFFEDAKLA SQELEITLTG RDAGEPERVP
     MCGVPFHAAD SYISKLIEKG YKVAICEQVE DPKVTKGIVK REVIRVITPG TLMDGSMLSE
     KDNNYLVAIS QTSSNNCGMA VADLSTGLFQ VTEMEGHWSL ESLLDEILRL TPREVLLTPD
     LKKHEKTVQA FNFLPSTVFT TLEETQQVSD YIELLNNQFG QKVSAVYKDR PAVCMAAGIL
     LQYLINTQKR QLNHITEITA YSPRAYMMLD GIARRNLEIS KSLRDGDKRG TLLWVLDATK
     TAMGGRMLKN WLEQPLIDTL KIQERLDAVE ELVNSILLRE EISGALKQIY DLERLAARAA
     YGSANGRDMI ALRGSLEKLP FIHDALAAVS STRLKRIYTE FNTLSDLRKV LDLALAENPP
     VSLRDGGLIK DGFDQEVDQL RNAARDGKTW LAGLEAREKE NTGIKNLKVG FNKVFGYYLE
     VTRANLSMVP EYYQRRQTLA NAERFITPEL KEYESMILGA EDRLVELEYN LFVAIRAKVA
     AEVSSIQKTA ALLSEIDALV SLAEVAVRNG FVRPEVTDNG IIEIKDGRHP VVENTQGLGG
     FVPNDTYLDI KEERLCLITG PNMGGKSTYQ RQVALIVLMA QVGSFVPAQR ARIGIVDRIF
     ARVGASDDLT SGQSTFMVEM YETKQIIDHA TAKSLVIIDE LGRGTSNLEG MAIAQSVIEF
     LHDEVGCRTL FSTHYHELAE LEGLLRGLKN YATAVKEQGD EVVFLRKVVR SKASKSYGVH
     CARLAGLPTS IIRRASELVM QLEFHQRAAQ EVVAGKTQIA AASEQLAMFT PQEDQVKEEI
     LALNLTNMTP LESLNFLDNL QKRLREMQ