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Reviewed, UniProtKB/Swiss-Prot P06710 (DPO3X_ECOLI)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA polymerase III subunit tau
    EC=2.7.7.7
Cleaved into the following chain:
    1- Recommended name:
            DNA polymerase III subunit gamma
Gene names
Name: dnaX
Synonyms: dnaZ, dnaZX
Ordered Locus Names: b0470, JW0459
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. This DNA polymerase also exhibits 3' to 5' exonuclease activity.

The tau chain serves as a scaffold to help in the dimerizaton of the core complex.

The gamma chain seems to interact with the delta subunit to transfer the beta subunit on the DNA.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

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].

Miscellaneous

The production of the two protein products from this region is due to programmed ribosomal frameshifting.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplAP0A7L01EBI-549140,EBI-543771

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643DNA polymerase III subunit tau
PRO_0000007360
Chain1 – 431431DNA polymerase III subunit gamma
PRO_0000007361

Regions

Nucleotide binding45 – 528ATP Potential

Secondary structure

.............................................................................. 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06710-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D2028BD99E375150

FASTA64371,138
        10         20         30         40         50         60 
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK 

        70         80         90        100        110        120 
GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF 

       130        140        150        160        170        180 
KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV 

       190        200        210        220        230        240 
EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM 

       250        260        270        280        290        300 
LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA 

       310        320        330        340        350        360 
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH 

       370        380        390        400        410        420 
PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ 

       430        440        450        460        470        480 
RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA 

       490        500        510        520        530        540 
TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA 

       550        560        570        580        590        600 
LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL 

       610        620        630        640 
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI 

« Hide

References

« Hide 'large scale' references
[1]"The adjacent dnaZ and dnaX genes of Escherichia coli are contained within one continuous open reading frame."
Flower A.M., McHenry C.S.
Nucleic Acids Res. 14:8091-8101(1986) [PubMed: 3534795] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / JM109 / ATCC 53323.
[2]"Nucleotide sequence of the Escherichia coli replication gene dnaZX."
Yin K.-C., Blinkowa A.L., Walker J.R.
Nucleic Acids Res. 14:6541-6549(1986) [PubMed: 3018672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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.
[4]"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 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III gamma subunit from within the tau subunit reading frame."
Blinkowa A.L., Walker J.R.
Nucleic Acids Res. 18:1725-1729(1990) [PubMed: 2186364] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT.
[7]"The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting."
Flower A.M., McHenry C.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3713-3717(1990) [PubMed: 2187190] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT.
[8]"Translational frameshifting generates the gamma subunit of DNA polymerase III holoenzyme."
Tsuchihashi Z., Kornberg A.
Proc. Natl. Acad. Sci. U.S.A. 87:2516-2520(1990) [PubMed: 2181440] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT.
[9]"Accessory protein function in the DNA polymerase III holoenzyme from E. coli."
O'Donnell M.
Bioessays 14:105-111(1992) [PubMed: 1575709] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

X04487 Genomic DNA. Translation: CAA28174.1.
X04487 Genomic DNA. Translation: CAA28175.1. Different initiation.
X04275 Genomic DNA. Translation: CAA27827.1.
U82664 Genomic DNA. Translation: AAB40224.1.
U00096 Genomic DNA. Translation: AAC73572.1.
AP009048 Genomic DNA. Translation: BAE76249.1.
M38777 Genomic DNA. Translation: AAA23457.1.
PIRDJEC3G. A25549.
RefSeqAP_001119.1.
NP_415003.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JR3X-ray2.70A/B/C1-373[»]
1NJFX-ray2.30A/B/C/D1-243[»]
1NJGX-ray2.20A/B1-243[»]
1XXHX-ray3.45B/C/D/G/H/I1-373[»]
1XXIX-ray4.10B/C/D/G/H/I1-368[»]
2AYANMR-A499-625[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9464N.
IntActP06710. 21 interactions.

2-D gel databases

ECO2DBASEH052.0. 6TH EDITION.
H080.0. 6TH EDITION.

Genome annotation databases

GeneID945105.
GenomeReviewsGene locus JW0459 in contig AP009048_GR.
Gene locus b0470 in contig U00096_GR.
KEGGecj:JW0459.
eco:b0470.

Organism-specific databases

EchoBASEEB0241.
EcoGeneEG10245. dnaX.
CMRSearch...

Phylogenomic databases

HOGENOMP06710.
OMAP06710. HAADGSM.

Enzyme and pathway databases

BioCycEcoCyc:EG10245-MON.
EcoCyc:MON0-2383.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR001270. Chaprnin_clpA/B.
IPR012763. DnaX_N.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
TIGRFAMsTIGR02397. dnaX_nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPO3X_ECOLI
AccessionPrimary (citable) accession number: P06710
Secondary accession number(s): Q2MBV7, Q47721
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents