ID   MUTS_ACIAD              Reviewed;         881 AA.
AC   Q6FC54;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=ACIAD1500;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG68357.1; -; Genomic_DNA.
DR   RefSeq; WP_004925309.1; NC_005966.1.
DR   AlphaFoldDB; Q6FC54; -.
DR   SMR; Q6FC54; -.
DR   STRING; 62977.ACIAD1500; -.
DR   EnsemblBacteria; CAG68357; CAG68357; ACIAD1500.
DR   GeneID; 45233906; -.
DR   KEGG; aci:ACIAD1500; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_4_0_6; -.
DR   OMA; TPMMAQY; -.
DR   OrthoDB; 15991at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06920-MON; -.
DR   Proteomes; UP000000430; 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..881
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_0000224343"
FT   BINDING         632..639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   881 AA;  98577 MW;  40CDADEA4E5A3F90 CRC64;
     MNSTETMADL SSYTPMMQQY FKVKLEHQHA LLFYRMGDFY ELFFDDARKA AKLLGITLTH
     RGKANGEPIP MAGVPYHAAE GYLARLVRAG QTVAICEQVG EGENAGSRCK APMERKVVRI
     ITPGTITDDA LLGSYQSSNL VALCIQQNKI GIALLDLSAS IFKVQQHEFK TEQLYIELAR
     LMPSEIVVDE DLVDQNILEQ IKKQIECSIT KRPNVDFNLN NAQKTLCDQF GVTTLSGFGI
     DHLPLAKAAA AALIHYAKET QKTALPHIRS IQLEQSTDFI ALDPITRRNL EIIDPLFEHG
     TSLFNLINDC QTAMGGRLLS RILMQPIRDT AILDARLDAT EQLLIGYHES PVRLVLKEIG
     DIERVLSRVA LGTARPRDLV QLRQACAQIP FLRHALLPAI QTKSSKLLNE LDHELGDFKD
     LHQLLLSAIV ENPPVLLRDG NVIAEGYDAE LDELRKIRDH AGQFLVDLEI KERESSGIPT
     LKIGYNRVSG YYIELTRAQA EQAPAYYIRR QTLKNAERYI TPELKSFEDK VLSSESRALA
     REKLLFESLL ETLKKNIANL QMMSSAIAQI DVLANFAHQA RLQNWNRPDF SPEIGIKIHD
     GRHPVVEALS KTPYTPNDTF LDSQHRMAII TGPNMGGKST FMRQTALISL LAYCGSYVPA
     KSAKLGPIDR IFTRIGSADD LSTGKSTFMV EMTETSQILH HATHQSLVLM DEVGRGTSTY
     DGLSLAWACV LDLTKRIKCL CLFATHYFEL TELGSESAID NYHVTAKEMN GNLILLHKVQ
     HGPASQSHGL QVAKLAGIPA SVIKEAQKRL KILEKQQQQY FQTAVQNDLF AIPELPQIDE
     TKIEIKKTSP VLDHLKQLDV DSLTPRQALE ALYQLKDQLE H