MUTS_SALTY
ID MUTS_SALTY Reviewed; 855 AA.
AC P0A1Y0; P10339;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA mismatch repair protein MutS;
GN Name=mutS; OrderedLocusNames=STM2909;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5.
RX PubMed=3275609; DOI=10.1128/jb.170.1.197-202.1988;
RA Haber L.T., Pang P.P., Sobell D.I., Mankovich J.A., Walker G.C.;
RT "Nucleotide sequence of the Salmonella typhimurium mutS gene required for
RT mismatch repair: homology of MutS and HexA of Streptococcus pneumoniae.";
RL J. Bacteriol. 170:197-202(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7783645; DOI=10.1111/j.1365-2958.1995.tb02382.x;
RA Mills D.M., Bajaj V., Lee C.A.;
RT "A 40 kb chromosomal fragment encoding Salmonella typhimurium invasion
RT genes is absent from the corresponding region of the Escherichia coli K-12
RT chromosome.";
RL Mol. Microbiol. 15:749-759(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP MUTAGENESIS, AND ATP-BINDING.
RX PubMed=1651234; DOI=10.1002/j.1460-2075.1991.tb07815.x;
RA Haber L.T., Walker G.C.;
RT "Altering the conserved nucleotide binding motif in the Salmonella
RT typhimurium MutS mismatch repair protein affects both its ATPase and
RT mismatch binding activities.";
RL EMBO J. 10:2707-2715(1991).
RN [5]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT IN 394-425.
RX PubMed=7903399; DOI=10.1006/jmbi.1993.1666;
RA Claverie J.-M.;
RT "Detecting frame shifts by amino acid sequence comparison.";
RL J. Mol. Biol. 234:1140-1157(1993).
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.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27167.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA80578.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M18965; AAA27167.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U16303; AAA80578.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE006468; AAL21789.1; -; Genomic_DNA.
DR PIR; A28668; A28668.
DR RefSeq; NP_461830.1; NC_003197.2.
DR RefSeq; WP_001005807.1; NC_003197.2.
DR AlphaFoldDB; P0A1Y0; -.
DR SMR; P0A1Y0; -.
DR STRING; 99287.STM2909; -.
DR PaxDb; P0A1Y0; -.
DR EnsemblBacteria; AAL21789; AAL21789; STM2909.
DR GeneID; 1254432; -.
DR KEGG; stm:STM2909; -.
DR PATRIC; fig|99287.12.peg.3063; -.
DR HOGENOM; CLU_002472_4_0_6; -.
DR OMA; TPMMAQY; -.
DR PhylomeDB; P0A1Y0; -.
DR BioCyc; SENT99287:STM2909-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..855
FT /note="DNA mismatch repair protein MutS"
FT /id="PRO_0000115132"
FT BINDING 616..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 622
FT /note="K->A: Defective in mismatch repair; ATPase activity
FT reduced 6-fold."
FT /evidence="ECO:0000269|PubMed:1651234"
FT CONFLICT 361..362
FT /note="TA -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 855 AA; 95407 MW; 804BEB131BCD2F6F CRC64;
MNESFDKDFS NHTPMMQQYL KLKAQHPEIL LFYRMGDFYE LFYDDAKRAS QLLDISLTKR
GASAGEPIPM AGIPHHAVEN YLAKLVNQGE SVAICEQIGD PATSKGPVER KVVRIVTPGT
ISDEALLQER QDNLLAAIWQ DGKGYGYATL DISSGRFRLS EPADRETMAA ELQRTNPAEL
LYAEDFAEMA LIEGRRGLRR RPLWEFEIDT ARQQLNLQFG TRDLVGFGVE NASRGLCAAG
CLLQYVKDTQ RTSLPHIRSI TMERQQDSII MDAATRRNLE ITQNLAGGVE NTLAAVLDCT
VTPMGSRMLK RWLHMPVRNT DILRERQQTI GALQDTVSEL QPVLRQVGDL ERILARLALR
TARPRDLARM RHAFQQLPEL HAQLETVDSA PVQALRKKMG DFAELRDLLE RAIIDAPPVL
VRDGGVIAPG YHEELDEWRA LADGATDYLD RLEIRERERT GLDTLKVGYN AVHGYYIQIS
RGQSHLAPIN YVRRQTLKNA ERYIIPELKE YEDKVLTSKG KALALEKQLY DELFDLLLPH
LADLQQSANA LAELDVLVNL AERAWTLNYT CPTFTDKPGI RITEGRHPVV EQVLNEPFIA
NPLNLSPQRR MLIITGPNMG GKSTYMRQTA LIALLAYIGS YVPAQNVEIG PIDRIFTRVG
AADDLASGRS TFMVEMTETA NILHNATENS LVLMDEIGRG TSTYDGLSLA WACAENLANK
IKALTLFATH YFELTQLPEK MEGVANVHLD ALEHGDTIAF MHSVQDGAAS KSYGLAVAAL
AGVPKEVIKR ARQKLRELES ISPNAAATQV DGTQMSLLAA PEETSPAVEA LENLDPDSLT
PRQALEWIYR LKSLV
