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dnaE DNA polymerase III subunit alpha [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944877, updated on 30-Jul-2025
Official Symbol
dnaE
Official Full Name
DNA polymerase III subunit alpha
Primary source
ECOCYC:EG10238
Locus tag
b0184
See related
ASAP:ABE-0000624
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
ECK0183; polC; sdgC
Summary
Has a PHP domin, like YcdX. [More information is available at EcoGene: EG10238]. The alpha subunit of DNA polymerase III catalyzes the polymerase activity of the holoenzyme complex . [More information is available at EcoCyc: EG10238].
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Sequence:
NC_000913.3 (205126..208608)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene acyl- Neighboring gene lipid A disaccharide synthase Neighboring gene RNase HII Neighboring gene acetyl-CoA carboxyltransferase subunit alpha Neighboring gene lysine decarboxylase 2

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Determination of the precise location and orientation of the Escherichia coli dnaE gene. Shepard D, et al. J Bacteriol, 1984 May. PMID 6327605, Free PMC Article
  2. Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. Wing RA, et al. J Mol Biol, 2008 Oct 17. PMID 18691598, Free PMC Article
  3. Differential effects of cisplatin and MNNG on dna mutants of Escherichia coli. Calmann MA, et al. Mutat Res, 2005 Oct 15. PMID 16144703, Free PMC Article
  4. Distinct double- and single-stranded DNA binding of E. coli replicative DNA polymerase III alpha subunit. McCauley MJ, et al. ACS Chem Biol, 2008 Sep 19. PMID 18652472, Free PMC Article
  5. Deoxyribonucleic acid synthesis in cell-free extracts. IV. Purification and catalytic properties of deoxyribonucleic acid polymerase III. Kornberg T, et al. J Biol Chem, 1972 Sep 10. PMID 4560196

See all (135) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. results support a model in which the pol and exo activities of pol III core are effectively independent, and in which recognition of the 3' end of the primer by either alpha or epsilon is governed by the primer stability.
    Title: Single-molecule mechanochemical characterization of E. coli pol III core catalytic activity.
  2. Mutation in PHP domain of Pol III alpha ablated interaction with the proofreading subunit.
    Title: DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection.
  3. Data show that the tau (tau), alpha (alpha), epsilon (epsilon), and theta (theta;) subunits of DNA Polymerase III can be assembled in vivo, yielding the trimeric tau3alpha3epsilon3theta;3 complex.
    Title: Simultaneous ternary extension of DNA catalyzed by a trimeric replicase assembled in vivo.
  4. The results suggest that competition between UmuD and ssDNA for DNA polymerase III alpha binding is a new mechanism for polymerase exchange.
    Title: Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.
  5. The PHP domain is a major structural element in Pol III and its integrity modulates both the stability and activity of the polymerase.
    Title: A structural role for the PHP domain in E. coli DNA polymerase III.
  6. Authors demonstrate for the first time that the major DNA polymerases (Pol I and Pol III) and DNA ligase are directly involved with oligo recombination.
    Title: Bacterial DNA polymerases participate in oligonucleotide recombination.
  7. Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB
    Title: [Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB].
  8. A structural model of the alphaepsilontheta;:beta2 replicase complex reveals a compact, but still flexible, structure of the complex.
    Title: Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.
  9. Authors report that DNA pol III incorporates 8-oxo-dGTP approximately 20 times more efficiently opposite template A compared with template C.
    Title: Escherichia coli DNA polymerase III is responsible for the high level of spontaneous mutations in mutT strains.
  10. Authors propose that the interaction between DNA polymerase III alpha and UmuD contributes to the transition between replicative and translesion synthesis polymerases by removing DNA polymerase III alpha from the beta clamp.
    Title: Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.
Submit: New GeneRIF Correction See all GeneRIFs (13)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
NOT enables 3'-5' exonuclease activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA polymerase activity IEA
Inferred from Electronic Annotation
more info
  
enables DNA-directed DNA polymerase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables DNA-directed DNA polymerase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA-directed DNA polymerase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity, acting on a nucleic acid IEA
Inferred from Electronic Annotation
more info
  
enables nucleic acid binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotidyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in DNA biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA replication IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA-templated DNA replication NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in lagging strand elongation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in leading strand elongation IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
part_of DNA polymerase III complex NAS
Non-traceable Author Statement
more info
 PubMed 
part_of DNA polymerase III, core complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of DNA polymerase III, core complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of replisome NAS
Non-traceable Author Statement
more info
 PubMed 
Preferred Names
DNA polymerase III subunit alpha
NP_414726.1

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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
    205126..208608
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414726.1 DNA polymerase III subunit alpha

    See identical proteins and their annotated locations for NP_414726.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A6M9X2B0, W1X3D1
    Conserved Domains (1) summary
    PRK05673
    Location:5 → 1151
    dnaE; DNA polymerase III subunit alpha; Validated
Nucleotide Protein
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