DNA polymerase III subunit epsilon

Details

Name
DNA polymerase III subunit epsilon
Synonyms
  • 2.7.7.7
  • mutD
Gene Name
dnaQ
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0004894|DNA polymerase III subunit epsilon
MSTAITRQIVLDTETTGMNQIGAHYEGHKIIEIGAVEVVNRRLTGNNFHVYLKPDRLVDP
EAFGVHGIADEFLLDKPTFAEVADEFMDYIRGAELVIHNAAFDIGFMDYEFSLLKRDIPK
TNTFCKVTDSLAVARKMFPGKRNSLDALCARYEIDNSKRTLHGALLDAQILAEVYLAMTG
GQTSMAFAMEGETQQQQGEATIQRIVRQASKLRVVFATDEEIAAHEARLDLVQKKGGSCL
WRA
Number of residues
243
Molecular Weight
27098.7
Theoretical pI
5.63
GO Classification
Functions
DNA binding / DNA-directed DNA polymerase activity / exonuclease activity / metal ion binding
Processes
DNA replication proofreading / nucleic acid phosphodiester bond hydrolysis
Components
DNA polymerase III, core complex
General Function
Metal ion binding
Specific Function
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0016807|DNA polymerase III subunit epsilon (dnaQ)
ATGAGCACTGCAATTACACGCCAGATCGTTCTCGATACCGAAACCACCGGTATGAACCAG
ATTGGTGCGCACTATGAAGGCCACAAGATCATTGAGATTGGTGCCGTTGAAGTGGTGAAC
CGTCGCCTGACGGGCAATAACTTCCATGTTTATCTCAAACCCGATCGGCTGGTGGATCCG
GAAGCCTTTGGCGTACATGGTATTGCCGATGAATTTTTGCTCGATAAGCCCACGTTTGCC
GAAGTAGCCGATGAGTTCATGGACTATATTCGCGGCGCGGAGTTGGTGATCCATAACGCA
GCGTTCGATATCGGCTTTATGGACTACGAGTTTTCGTTGCTTAAGCGCGATATTCCGAAG
ACCAATACTTTCTGTAAGGTCACCGATAGCCTTGCGGTGGCGAGGAAAATGTTTCCCGGT
AAGCGCAACAGCCTCGATGCGTTATGTGCTCGCTACGAAATAGATAACAGTAAACGAACG
CTGCACGGGGCATTACTCGATGCCCAGATCCTTGCGGAAGTTTATCTGGCGATGACCGGT
GGTCAAACGTCGATGGCTTTTGCGATGGAAGGAGAGACACAACAGCAACAAGGTGAAGCA
ACAATTCAGCGCATTGTACGTCAGGCAAGTAAGTTACGCGTTGTTTTTGCGACAGATGAA
GAGATTGCAGCTCATGAAGCCCGTCTCGATCTGGTGCAGAAGAAAGGCGGAAGTTGCCTC
TGGCGAGCATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP03007
UniProtKB Entry NameDPO3E_ECOLI
GenBank Gene IDX04027
General References
  1. Cox EC, Horner DL: DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene. J Mol Biol. 1986 Jul 5;190(1):113-7. [PubMed:3023634]
  2. Maki H, Horiuchi T, Sekiguchi M: Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promoter regions. Proc Natl Acad Sci U S A. 1983 Dec;80(23):7137-41. [PubMed:6316347]
  3. Takano K, Nakabeppu Y, Maki H, Horiuchi T, Sekiguchi M: Structure and function of dnaQ and mutD mutators of Escherichia coli. Mol Gen Genet. 1986 Oct;205(1):9-13. [PubMed:3540531]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [PubMed:9278503]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed:16738553]
  6. O'Donnell M: Accessory protein function in the DNA polymerase III holoenzyme from E. coli. Bioessays. 1992 Feb;14(2):105-11. [PubMed:1575709]
  7. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [PubMed:9298644]
  8. Hamdan S, Carr PD, Brown SE, Ollis DL, Dixon NE: Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure. 2002 Apr;10(4):535-46. [PubMed:11937058]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01643Thymidine monophosphateexperimentalunknownDetails