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DnaQ

Protein FULL name:

DNA polymerase III epsilon subunit [Escherichia coli].


DnaQ (Escherichia coli strain K-12 substr. MG1655) is product of expression of dnaQ gene.


DnaQ is involved in:

MMR in Escherichia coli strain K-12 substr. MG1655
     
DDS in Escherichia coli strain K-12 substr. MG1655
     


Keywords:



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.

CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

COFACTOR: Binds 2 divalent metal cations. Magnesium or manganese.

SUBUNIT: The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha,epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different dnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi- beta[4].

INTERACTION: P10443:dnaE; NbExp=3; IntAct=EBI-549131, EBI-549111; P0ABS8:holE; NbExp=1; IntAct=EBI-549131, EBI-549182;

SEQUENCE CAUTION: Sequence=AAB08637.1; Type=Erroneous initiation;


This protein can be a part of a given complexes:
NCBI GenPept GI number(s): 147679
Species: Escherichia coli

Links to other databases:

Database ID Link
Uniprot P03007 P03007
PFAM: - P03007 (Link - using uniprot id)
InterPro: - P03007 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSTAITRQIVLDTETTGMNQIGAHYEGHKIIEIGAVEVVNRRLTGNNFHV
YLKPDRLVDPEAFGVHGIADEFLLDKPTFAEVADEFMDYIRGAELVIHNA
AFDIGFMDYEFSLLKRDIPKTNTFCKVTDSLAVARKMFPGKRNSLDALCA
RYEIDNSKRTLHGALLDAQILAEVYLAMTGGQTSMAFAMEGETQQQQGEA
TIQRIVRQASKLRVVFATDEEIAAHEARLDLVQKKGGSCLWRA

References:

Title Authors Journal
Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promoter regions. Maki H, Horiuchi T, Sekiguchi M Proc Natl Acad Sci U S A Dec. 1, 1983
DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene. Cox EC, Horner DL J Mol Biol July 5, 1986
Structure and function of dnaQ and mutD mutators of Escherichia coli. Takano K, Nakabeppu Y, Maki H, Horiuchi T, Sekiguchi M Mol Gen Genet Oct. 1, 1986
Accessory protein function in the DNA polymerase III holoenzyme from E. coli. O'Donnell M Bioessays Jan. 1, 1992
The complete genome sequence of Escherichia coli K-12. 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 Science Sept. 5, 1997
Structural basis for proofreading during replication of the Escherichia coli chromosome. Hamdan S, Carr PD, Brown SE, Ollis DL, Dixon NE Structure April 1, 2002
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T Mol Syst Biol Jan. 1, 2006


Last modification of this entry: Oct. 12, 2010.

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