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
- FunctionsDNA binding / DNA-directed DNA polymerase activity / exonuclease activity / metal ion bindingProcessesDNA replication proofreading / nucleic acid phosphodiester bond hydrolysisComponentsDNA 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
- RNase_T (PF00929)
- 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
Resource Link UniProtKB ID P03007 UniProtKB Entry Name DPO3E_ECOLI GenBank Gene ID X04027 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- O'Donnell M: Accessory protein function in the DNA polymerase III holoenzyme from E. coli. Bioessays. 1992 Feb;14(2):105-11. [Article]
- 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. [Article]
- 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. [Article]