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P06710

- DPO3X_ECOLI

UniProt

P06710 - DPO3X_ECOLI

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Protein
DNA polymerase III subunit tau
Gene
dnaX, dnaZ, dnaZX, b0470, JW0459
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 528ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: EcoliWiki
  3. DNA binding Source: InterPro
  4. DNA polymerase processivity factor activity Source: EcoliWiki
  5. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  6. identical protein binding Source: IntAct
  7. nucleoside-triphosphatase activity Source: EcoliWiki
  8. protein binding Source: IntAct

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA replication Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit tau (EC:2.7.7.7)
Alternative name(s):
DNA polymerase III subunit gamma
Gene namesi
Name:dnaX
Synonyms:dnaZ, dnaZX
Ordered Locus Names:b0470, JW0459
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10245. dnaX.

Subcellular locationi

GO - Cellular componenti

  1. DNA polymerase III, clamp loader complex Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 643642DNA polymerase III subunit tau
PRO_0000007360Add
BLAST

Proteomic databases

PaxDbiP06710.
PRIDEiP06710.

Expressioni

Gene expression databases

GenevestigatoriP06710.

Interactioni

Subunit structurei

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].

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-549140,EBI-549140
bglGP119893EBI-549140,EBI-545674
dnaBP0ACB02EBI-549140,EBI-548978
dnaEP1044310EBI-549140,EBI-549111
dnaNP0A9884EBI-549140,EBI-542385
dnaQP030074EBI-549140,EBI-549131
ficP206052EBI-549140,EBI-1132602
holAP286305EBI-6464728,EBI-549153
holBP2863117EBI-549140,EBI-549161
holCP2890513EBI-549140,EBI-549169
holDP2863218EBI-549140,EBI-549176
ssbP0AGE02EBI-549140,EBI-1118620

Protein-protein interaction databases

DIPiDIP-9464N.
IntActiP06710. 32 interactions.
MINTiMINT-1222776.
STRINGi511145.b0470.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94
Helixi15 – 173
Helixi22 – 3413
Beta strandi39 – 446
Beta strandi46 – 505
Helixi51 – 6313
Helixi77 – 837
Beta strandi88 – 947
Turni95 – 973
Helixi98 – 1003
Helixi101 – 1099
Beta strandi111 – 1133
Beta strandi116 – 12611
Helixi128 – 1303
Helixi133 – 14412
Beta strandi150 – 1578
Helixi159 – 1613
Helixi164 – 1674
Beta strandi170 – 1745
Helixi180 – 19314
Helixi200 – 21011
Helixi214 – 22512
Turni226 – 2294
Beta strandi230 – 2323
Helixi234 – 2407
Helixi248 – 25710
Helixi261 – 27414
Helixi278 – 29417
Turni295 – 2973
Helixi299 – 3013
Turni304 – 3063
Helixi307 – 31812
Helixi322 – 33817
Turni339 – 3413
Beta strandi342 – 3443
Helixi345 – 35814
Beta strandi361 – 3633
Helixi507 – 52014
Helixi522 – 5309
Helixi535 – 5417
Beta strandi543 – 5475
Beta strandi549 – 5568
Helixi558 – 5603
Turni561 – 5633
Helixi566 – 58015
Beta strandi585 – 5906
Helixi599 – 62022

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP06710.
SMRiP06710. Positions 3-368, 499-625.

Miscellaneous databases

EvolutionaryTraceiP06710.

Family & Domainsi

Sequence similaritiesi

Belongs to the DnaX/STICHEL family.

Phylogenomic databases

eggNOGiCOG2812.
HOGENOMiHOG000083934.
KOiK02343.
OMAiQRHLNSP.
OrthoDBiEOG6WQD76.
PhylomeDBiP06710.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR001270. 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.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF12169. DNA_pol3_gamma3. 1 hit.
PF12168. DNA_pol3_tau_4. 1 hit.
PF12170. DNA_pol3_tau_5. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02397. dnaX_nterm. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG    50
KTSIARLLAK GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK 100
VEDTRDLLDN VQYAPARGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEHV 150
KFLLATTDPQ KLPVTILSRC LQFHLKALDV EQIRHQLEHI LNEEHIAHEP 200
RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM LGTLDDDQAL 250
SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA 300
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE 350
MTLLRALAFH PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA 400
PTVPLPETTS QVLAARQQLQ RVQGATKAKK SEPAAATRAR PVNNAALERL 450
ASVTDRVQAR PVPSALEKAP AKKEAYRWKA TTPVMQQKEV VATPKALKKA 500
LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA LNAWKEESDN 550
AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL 600
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI 643

Note: Produced by full-length translation of the dnaX gene.

Length:643
Mass (Da):71,138
Last modified:January 1, 1988 - v1
Checksum:iD2028BD99E375150
GO
Isoform gamma (identifier: P06710-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:431
Mass (Da):47,545
Checksum:i8177A07F31BC86E3
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei431 – 4311S → E in isoform gamma.
VSP_042848
Alternative sequencei432 – 643212Missing in isoform gamma.
VSP_042849Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA25549. DJEC3G.
RefSeqiNP_415003.1. NC_000913.3.
YP_488761.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73572; AAC73572; b0470.
BAE76249; BAE76249; BAE76249.
GeneIDi12930852.
945105.
KEGGiecj:Y75_p0457.
eco:b0470.
PATRICi32116097. VBIEscCol129921_0490.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A25549. DJEC3G.
RefSeqi NP_415003.1. NC_000913.3.
YP_488761.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JR3 X-ray 2.70 A/B/C 1-373 [» ]
1NJF X-ray 2.30 A/B/C/D 1-243 [» ]
1NJG X-ray 2.20 A/B 1-243 [» ]
1XXH X-ray 3.45 B/C/D/G/H/I 1-373 [» ]
1XXI X-ray 4.10 B/C/D/G/H/I 1-368 [» ]
2AYA NMR - A 499-625 [» ]
3GLF X-ray 3.39 B/C/D/G/H/I 1-373 [» ]
3GLG X-ray 3.25 B/C/D/G/H/I 1-373 [» ]
3GLH X-ray 3.89 B/C/D/G/H/I/L/M/N 1-373 [» ]
3GLI X-ray 3.50 B/C/D/G/H/I 1-373 [» ]
ProteinModelPortali P06710.
SMRi P06710. Positions 3-368, 499-625.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9464N.
IntActi P06710. 32 interactions.
MINTi MINT-1222776.
STRINGi 511145.b0470.

Chemistry

BindingDBi P06710.

Proteomic databases

PaxDbi P06710.
PRIDEi P06710.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73572 ; AAC73572 ; b0470 .
BAE76249 ; BAE76249 ; BAE76249 .
GeneIDi 12930852.
945105.
KEGGi ecj:Y75_p0457.
eco:b0470.
PATRICi 32116097. VBIEscCol129921_0490.

Organism-specific databases

EchoBASEi EB0241.
EcoGenei EG10245. dnaX.

Phylogenomic databases

eggNOGi COG2812.
HOGENOMi HOG000083934.
KOi K02343.
OMAi QRHLNSP.
OrthoDBi EOG6WQD76.
PhylomeDBi P06710.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P06710.
PROi P06710.

Gene expression databases

Genevestigatori P06710.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR001270. 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.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF12169. DNA_pol3_gamma3. 1 hit.
PF12168. DNA_pol3_tau_4. 1 hit.
PF12170. DNA_pol3_tau_5. 1 hit.
[Graphical view ]
PRINTSi PR00300. CLPPROTEASEA.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR02397. dnaX_nterm. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDPO3X_ECOLI
AccessioniPrimary (citable) accession number: P06710
Secondary accession number(s): Q2MBV7, Q47721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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