MUTS_CLOD6
ID MUTS_CLOD6 Reviewed; 947 AA.
AC Q187T6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=CD630_19770;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ68852.2; -; Genomic_DNA.
DR RefSeq; WP_003435264.1; NZ_CP010905.2.
DR RefSeq; YP_001088483.2; NC_009089.1.
DR AlphaFoldDB; Q187T6; -.
DR SMR; Q187T6; -.
DR STRING; 272563.CD630_19770; -.
DR PRIDE; Q187T6; -.
DR EnsemblBacteria; CAJ68852; CAJ68852; CD630_19770.
DR KEGG; cdf:CD630_19770; -.
DR KEGG; pdc:CDIF630_02182; -.
DR PATRIC; fig|272563.120.peg.2074; -.
DR eggNOG; COG0249; Bacteria.
DR OMA; TPMMAQY; -.
DR PhylomeDB; Q187T6; -.
DR BioCyc; PDIF272563:G12WB-2119-MON; -.
DR Proteomes; UP000001978; 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..947
FT /note="DNA mismatch repair protein MutS"
FT /id="PRO_0000335142"
FT BINDING 620..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ SEQUENCE 947 AA; 108579 MW; 1C7D9F7394D55628 CRC64;
MQIDMNKLTP MMKQYLEVKN RYKDCILFFR LGDFYEMFFE DALVASKALE IALTGKACGL
EERAPMCGVP FHSANSYISK LVENGYKVAI GEQMEDPSTA KGIVRREVIR VITPGTVLDG
NLLENKKNNY LLSLYKDGTN IGLTYVDIST GETNATCLNE DKVIEEIAKI HPTEIIINDL
DFIEKLRDIA TVSNIYINES FSDNYLDINI LKEYFPDVYL QKLKFDDKGL IKSSLSILLN
YIYNTQKQIT SNINNINIYN SSEYMVLDMF TRTNLELTQT IRGNKKKGSL LHVLDKTSTA
MGGRLLRKYV EEPLINKSKI ENRLDVIEEI KDDFILREDL NDILKNIYDI ERICGKIAFE
RVTPKELIHL KNSIEKLPNL KDTINLSNAK ILKEYVSEMD KLDDIYNLID EAILEEPTIT
IKDGNIIKSD FSDELKELRE ISKNGAFLVK EIENREREKT GVKSLKIGFN KVFGYYIEIT
KANFKQAKLD ETYIRKQTLS NAERYITPEL KEIEEKILHA EEKIKSLEYE IFVEIRDTIY
KNIDRIQKVA KTIANIDVFV SLATVAHINN YVKPAINENN KLDIRNGRHP VVENIVGEEN
FVPNDTYLNR GENIINIITG PNMSGKSTYM RQTAIIALMA HIGSFVPAES ADIPILDRIF
TRVGASDDLS QGQSTFMVEM NEVSLILKNA TERSLVILDE IGRGTSTYDG ISLAWSIVEY
IQKNIRCKTL FATHYHELTD LEEEFKEVKN YSIAVKEDGE GIIFLRKIIP QGADKSYGIY
VAKLAKLPDE VIERAKYILK DLEKNHVYNS VAINGDKENN NIINSNLDEE LVKVNQSNFK
NKYESLKIEH ELIVKDYKHI KKDYDKLNSK FKALNDEVAL MKQNDDKEKI NQEDSVKEVA
LTQISFDSVN RDILSEEILN LDILNMTPLD AINSLYNLQR KAKEIKS