ID   MUTS_ALBFT              Reviewed;         882 AA.
AC   Q21XE3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=Rfer_1832;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD69560.1; -; Genomic_DNA.
DR   RefSeq; WP_011464128.1; NC_007908.1.
DR   AlphaFoldDB; Q21XE3; -.
DR   SMR; Q21XE3; -.
DR   STRING; 338969.Rfer_1832; -.
DR   EnsemblBacteria; ABD69560; ABD69560; Rfer_1832.
DR   KEGG; rfr:Rfer_1832; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_4_0_4; -.
DR   OMA; TPMMAQY; -.
DR   OrthoDB; 15991at2; -.
DR   Proteomes; UP000008332; 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..882
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_0000335213"
FT   BINDING         640..647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   882 AA;  96095 MW;  0EC6F1E376EB5383 CRC64;
     MQNEKTQSKK PSPVPAEHSP MMAQYFGLKA DYPDTLLFYR MGDFYELFFA DAEKAARLLN
     ITLTQRGQSA GQPVVMAGVP FHSVDTYLAR LIKLGESVAI CEQVGEVTGK GPVERKVVRV
     VTPGTLTDLE LLSDKSESML LAVHQGPRNT CGLAWLSVTQ GEVHLAECAV DDLAQWVLRI
     APGEIIFSAG TTPTFEARLR GAPLAGAVSV SVRPDWQFDA GLGEKKLLAQ LQAASLAPWQ
     AQDLPQAHAA AAALLGYAEH TQGQALTHIQ SVRVQRSDEL IDLPPTTRRN LELTQTLRGE
     DQPTLFSLLD TCMTGMGSRL LKNWLLEPRR DRGEAQQRLN AIAALQSGDA HTSRAGVWRQ
     LREQLKGSTD VERITARIAL RQVRPRELVA LQLTLQKTEL LTHTTRGLEV YLTQISGHLL
     APEACADLLA RAIDPEPAVL VRDGGVIASG FDAELDELRA IQTNCDGFLL DLEVREKART
     GIANLRVQFN KVHGFFIEVT QGQVDKVPDD YRRRQTLKNA ERFITPELKA FEDKALSAQE
     RALAREKWLY EQVLDQLQVF VPALTRVARA LATLDALCAL TERSLTLDWC APQFVKEPCL
     DITQGRHPVV QARLAETSSG AFIANDTRMG PKQRMQIITG PNMGGKSTYM RQIAVIVLLA
     SMGSYVPASA CRLGPIDAIH TRIGAADDLA NAQSTFMLEM LEAAQILIAA TPNSLVLMDE
     IGRGTSTFDG LALASSIATQ LHDKTQAYTL FATHYFELTE FPAQHHAAIN VHVSAAEAGR
     DIVFLHEIQP GPASKSYGIQ VARLAGMPAA VLNQARQTLA ALESQATQNQ AQVDLFAAPP
     ATETAADSAI ETAVAALNPD NLSPREALEA LYQLKKLASG KA