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P03007 (DPO3E_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase III subunit epsilon

EC=2.7.7.7
Gene names
Name:dnaQ
Synonyms:mutD
Ordered Locus Names:b0215, JW0205
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

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].

Sequence caution

The sequence AAB08637.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243DNA polymerase III subunit epsilon
PRO_0000105483

Sites

Active site1621Proton acceptor
Metal binding121Divalent metal cation 1; catalytic
Metal binding121Divalent metal cation 2; catalytic
Metal binding141Divalent metal cation 1; catalytic
Metal binding1671Divalent metal cation 1; catalytic
Binding site121Substrate
Binding site141Substrate
Binding site611Substrate
Binding site661Substrate
Binding site1671Substrate

Secondary structure

............................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03007 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 4211C9A00744964F

FASTA24327,099
        10         20         30         40         50         60 
MSTAITRQIV LDTETTGMNQ IGAHYEGHKI IEIGAVEVVN RRLTGNNFHV YLKPDRLVDP 

        70         80         90        100        110        120 
EAFGVHGIAD EFLLDKPTFA EVADEFMDYI RGAELVIHNA AFDIGFMDYE FSLLKRDIPK 

       130        140        150        160        170        180 
TNTFCKVTDS LAVARKMFPG KRNSLDALCA RYEIDNSKRT LHGALLDAQI LAEVYLAMTG 

       190        200        210        220        230        240 
GQTSMAFAME GETQQQQGEA TIQRIVRQAS KLRVVFATDE EIAAHEARLD LVQKKGGSCL 


WRA 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene."
Cox E.C., Horner D.L.
J. Mol. Biol. 190:113-117(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. 80:7137-7141(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure and function of dnaQ and mutD mutators of Escherichia coli."
Takano K., Nakabeppu Y., Maki H., Horiuchi T., Sekiguchi M.
Mol. Gen. Genet. 205:9-13(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"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 B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Accessory protein function in the DNA polymerase III holoenzyme from E. coli."
O'Donnell M.
Bioessays 14:105-111(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Structural basis for proofreading during replication of the Escherichia coli chromosome."
Hamdan S., Carr P.D., Brown S.E., Ollis D.L., Dixon N.E.
Structure 10:535-546(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-186 IN COMPLEX WITH METAL IONS AND SUBSTRATE ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04027 Genomic DNA. Translation: CAA27661.1.
K00985 Genomic DNA. Translation: AAA24564.1.
U70214 Genomic DNA. Translation: AAB08637.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73320.1.
AP009048 Genomic DNA. Translation: BAA77886.1.
PIRIQECQ. A64746.
RefSeqNP_414751.1. NC_000913.3.
YP_488512.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J53X-ray1.80A1-186[»]
1J54X-ray1.70A1-186[»]
1MGZmodel-A1-186[»]
2GUIX-ray1.60A2-186[»]
2IDOX-ray2.10A/C1-186[»]
2XY8NMR-A1-186[»]
4GX8X-ray1.70A/B/C/D209-243[»]
4GX9X-ray2.15A/B/C/D200-243[»]
ProteinModelPortalP03007.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9462N.
IntActP03007. 28 interactions.
MINTMINT-1222832.
STRING511145.b0215.

Chemistry

ChEMBLCHEMBL1075047.

2D gel databases

SWISS-2DPAGEP03007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73320; AAC73320; b0215.
BAA77886; BAA77886; BAA77886.
GeneID12933127.
946441.
KEGGecj:Y75_p0206.
eco:b0215.
PATRIC32115543. VBIEscCol129921_0217.

Organism-specific databases

EchoBASEEB0239.
EcoGeneEG10243. dnaQ.

Phylogenomic databases

eggNOGCOG0847.
HOGENOMHOG000258616.
KOK02342.
OMAGFMDHEF.
OrthoDBEOG696BTR.
PhylomeDBP03007.

Enzyme and pathway databases

BioCycEcoCyc:EG10243-MONOMER.
ECOL316407:JW0205-MONOMER.
MetaCyc:EG10243-MONOMER.

Gene expression databases

GenevestigatorP03007.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR006054. DnaQ.
IPR006309. DnaQ_proteo.
IPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00573. dnaq. 1 hit.
TIGR01406. dnaQ_proteo. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03007.
PROP03007.

Entry information

Entry nameDPO3E_ECOLI
AccessionPrimary (citable) accession number: P03007
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene