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mutS DNA mismatch repair protein MutS [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947206, updated on 4-Feb-2026
Official Symbol
mutS
Official Full Name
DNA mismatch repair protein MutS
Primary source
ECOCYC:EG10625
Locus tag
b2733
See related
ASAP:ABE-0008977
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ant; ECK2728; fdv; plm
Summary
MutS has weak ATPase activity and may be involved in recognizing the DNA mismatch. [More information is available at EcoGene: EG10625]. MutS is one of the components of the MutHLS complex. [More information is available at EcoCyc: EG10625].
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Sequence:
NC_000913.3 (2857093..2859654)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional activator FhlA Neighboring gene protein YgbA Neighboring gene phosphoprotein phosphatase 2 Neighboring gene DNA-binding transcriptional repressor YgbI

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Binding specificities of the mismatch binding protein, MutS, to oligonucleotides containing modified bases. Negishi K, et al. Nucleic Acids Res Suppl, 2001. PMID 12836344
  2. Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes. Castellano-Castillo M, et al. J Biol Inorg Chem, 2008 Aug. PMID 18491151
  3. Binding of MutS protein to oligonucleotides containing a methylated or an ethylated guanine residue, and correlation with mutation frequency. Taira K, et al. Mutat Res, 2008 Apr 2. PMID 18243250, Free PMC Article
  4. Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis. Blackwell LJ, et al. J Biol Chem, 2001 Sep 7. PMID 11454861
  5. The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition. Schofield MJ, et al. J Biol Chem, 2001 Dec 7. PMID 11602569

See all (158) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The selection process of licensing a DNA mismatch for repair.
    Title: The selection process of licensing a DNA mismatch for repair.
  2. Responses of DNA Mismatch Repair Proteins to a Stable G-Quadruplex Embedded into a DNA Duplex Structure.
    Title: Responses of DNA Mismatch Repair Proteins to a Stable G-Quadruplex Embedded into a DNA Duplex Structure.
  3. we observe that a single residue substitution (R168C) results in a high rate of head-to-tail (tandem) short sequence duplications, which are independent of existing sequence repeats. Finally, we show that the unique mutation spectrum of topA mutants enhances the emergence of antibiotic resistance in comparison to mismatch-repair (mutS) mutators, and leads to new resistance genotypes.
    Title: Point mutations in topoisomerase I alter the mutation spectrum in E. coli and impact the emergence of drug resistance genotypes.
  4. Sharp kinking of a coiled-coil in MutS allows DNA binding and release.
    Title: Sharp kinking of a coiled-coil in MutS allows DNA binding and release.
  5. Mechanism for verification of mismatched and homoduplex DNAs by nucleotides-bound MutS analyzed by molecular dynamics simulations has been reported.
    Title: Mechanism for verification of mismatched and homoduplex DNAs by nucleotides-bound MutS analyzed by molecular dynamics simulations.
  6. The assembly of an EcMutS-EcMutL-EcMutH search complex illustrates how sequential stable sliding clamps can modulate one-dimensional diffusion mechanics along the DNA to direct mismatch repair
    Title: Cascading MutS and MutL sliding clamps control DNA diffusion to activate mismatch repair.
  7. The structure captures MutS in the sliding clamp conformation, where tilting of the MutS subunits across each other pushes DNA into a new channel, and reorientation of the connector domain creates an interface for MutL with both MutS subunits.
    Title: MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.
  8. MutS and MutL trap recombination intermediates using mismatches formed in the heteroduplex region and secondary DNA structures in the displaced ssDNA, and recruit the UvrD helicase to resolve these trapped intermediates in a directional manner
    Title: Mismatch repair inhibits homeologous recombination via coordinated directional unwinding of trapped DNA structures.
  9. E. coli MutS has a binding activity specific for non-B form G4 DNA, but such binding appears independent of canonical heteroduplex repair activation.
    Title: G-quadruplex recognition activities of E. Coli MutS.
  10. The results confirm that specifically bound MutS bends DNA at the mismatch.
    Title: Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNA.
Submit: New GeneRIF Correction See all GeneRIFs (26)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ADP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP-dependent DNA damage sensor activity IEA
Inferred from Electronic Annotation
more info
  
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA binding, bending IDA
Inferred from Direct Assay
more info
 PubMed 
enables adenine/cytosine mispair binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables damaged DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables mismatched DNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables mismatched DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables mismatched DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in DNA damage response IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA damage response IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in DNA repair IEA
Inferred from Electronic Annotation
more info
  
involved_in mismatch repair IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in mismatch repair IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in mismatch repair IEA
Inferred from Electronic Annotation
more info
  
involved_in mismatch repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within regulation of DNA recombination IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of DNA recombination NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of mismatch repair complex IC
Inferred by Curator
more info
 PubMed 
Preferred Names
DNA mismatch repair protein MutS

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    2857093..2859654
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417213.1 DNA mismatch repair protein MutS

    See identical proteins and their annotated locations for NP_417213.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A377C3D5, A0AAN5ZJC4
    Conserved Domains (1) summary
    PRK05399
    Location:3 → 853
    PRK05399; DNA mismatch repair protein MutS; Provisional
Nucleotide Protein
Heading Accession and Version

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