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P06710 (DPO3X_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. Feed History...

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

Names and origin

Protein namesRecommended name:
DNA polymerase III subunit tau
EC=2.7.7.7
Alternative name(s):
DNA polymerase III subunit gamma
Gene names
Name:dnaX
Synonyms:dnaZ, dnaZX
Ordered Locus Names:b0470, JW0459
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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.

Isoform tau: serves as a scaffold to help in the dimerization of the core complex.

Isoform gamma: 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, isoform gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(isoform:gamma/tau)[3]-delta,delta', psi,chi-beta[4].

Sequence caution

The sequence CAA28175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: The production of the two protein products from this region is due to programmed ribosomal frameshifting. Frameshifting is about 40% efficient.
Isoform tau (identifier: P06710-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by full-length translation of the dnaX gene.
Isoform gamma (identifier: P06710-2)

The sequence of this isoform differs from the canonical sequence as follows:
     431-431: S → E
     432-643: Missing.
Note: Formed by programmed ribosomal frameshifting to a premature stop codon in the -1 frame at codon 430, the last residue is thus Glu and not Ser.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 643642DNA polymerase III subunit tau
PRO_0000007360

Regions

Nucleotide binding45 – 528ATP Potential

Natural variations

Alternative sequence4311S → E in isoform gamma.
VSP_042848
Alternative sequence432 – 643212Missing in isoform gamma.
VSP_042849

Secondary structure

1 ................................................................................... 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform tau [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

Isoform gamma [UniParc].

Checksum: 8177A07F31BC86E3
Show »

FASTA43147,545

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"DNA polymerase III holoenzyme of Escherichia coli. I. Purification and distinctive functions of subunits tau and gamma, the dnaZX gene products."
Maki S., Kornberg A.
J. Biol. Chem. 263:6547-6554(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13.
Strain: ATCC 33694 / HB101.
[7]"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] [Europe PMC] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT, ISOFORMS TAU AND GAMMA, PROTEIN SEQUENCE OF 428-431 (ISOFORM GAMMA).
[8]"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] [Europe PMC] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT, ISOFORMS TAU AND GAMMA.
Strain: K12 / JM103Y.
[9]"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] [Europe PMC] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT, ISOFORMS TAU AND GAMMA.
Strain: K12.
[10]"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.
[11]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
RefSeqNP_415003.1. NC_000913.2.
YP_488761.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3GLFX-ray3.39B/C/D/G/H/I1-373[»]
3GLGX-ray3.25B/C/D/G/H/I1-373[»]
3GLHX-ray3.89B/C/D/G/H/I/L/M/N1-373[»]
3GLIX-ray3.50B/C/D/G/H/I1-373[»]
ProteinModelPortalP06710.
SMRP06710. Positions 3-368, 499-625.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9464N.
IntActP06710. 24 interactions.
MINTMINT-1222776.
STRING511145.b0470.

Proteomic databases

PaxDbP06710.
PRIDEP06710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73572; AAC73572; b0470.
BAE76249; BAE76249; BAE76249.
GeneID12930852.
945105.
KEGGecj:Y75_p0457.
eco:b0470.
PATRIC32116097. VBIEscCol129921_0490.

Organism-specific databases

EchoBASEEB0241.
EcoGeneEG10245. dnaX.

Phylogenomic databases

eggNOGCOG2812.
HOGENOMHOG000083934.
KOK02343.
OMAVQLYYQT.
ProtClustDBPRK07994.

Enzyme and pathway databases

BioCycEcoCyc:EG10245-MONOMER.
EcoCyc:MONOMER0-2383.
ECOL316407:JW0459-MONOMER.

Gene expression databases

GenevestigatorP06710.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR001270. Chaprnin_ClpA/B.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR022001. DNA_pol3_tau_IV.
IPR022754. DNA_pol_III_gamma-3.
IPR012763. DNA_pol_III_sug/sutau.
IPR021029. DNA_pol_III_tau_dom-5.
[Graphical view]
PfamPF12169. DNA_pol3_gamma3. 1 hit.
PF12168. DNA_pol3_tau_4. 1 hit.
PF12170. DNA_pol3_tau_5. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF48019. Pol_clamp_load_C. 1 hit.
TIGRFAMsTIGR02397. dnaX_nterm. 1 hit.
ProtoNetSearch...

Other

BindingDBP06710.
EvolutionaryTraceP06710.

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: May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents