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P06710

- DPO3X_ECOLI

UniProt

P06710 - DPO3X_ECOLI

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Protein

DNA polymerase III subunit tau

Gene

dnaX

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 – 528ATPSequence Analysis

GO - Molecular functioni

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

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 tauPRO_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

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Helixi15 – 173Combined sources
Helixi22 – 3413Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 505Combined sources
Helixi51 – 6313Combined sources
Helixi77 – 837Combined sources
Beta strandi88 – 947Combined sources
Turni95 – 973Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 1099Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi116 – 12611Combined sources
Helixi128 – 1303Combined sources
Helixi133 – 14412Combined sources
Beta strandi150 – 1578Combined sources
Helixi159 – 1613Combined sources
Helixi164 – 1674Combined sources
Beta strandi170 – 1745Combined sources
Helixi180 – 19314Combined sources
Helixi200 – 21011Combined sources
Helixi214 – 22512Combined sources
Turni226 – 2294Combined sources
Beta strandi230 – 2323Combined sources
Helixi234 – 2407Combined sources
Helixi248 – 25710Combined sources
Helixi261 – 27414Combined sources
Helixi278 – 29417Combined sources
Turni295 – 2973Combined sources
Helixi299 – 3013Combined sources
Turni304 – 3063Combined sources
Helixi307 – 31812Combined sources
Helixi322 – 33817Combined sources
Turni339 – 3413Combined sources
Beta strandi342 – 3443Combined sources
Helixi345 – 35814Combined sources
Beta strandi361 – 3633Combined sources
Helixi507 – 52014Combined sources
Helixi522 – 5309Combined sources
Helixi535 – 5417Combined sources
Beta strandi543 – 5475Combined sources
Beta strandi549 – 5568Combined sources
Helixi558 – 5603Combined sources
Turni561 – 5633Combined sources
Helixi566 – 58015Combined sources
Beta strandi585 – 5906Combined sources
Helixi599 – 62022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06710.

Family & Domainsi

Sequence similaritiesi

Belongs to the DnaX/STICHEL family.Curated

Phylogenomic databases

eggNOGiCOG2812.
HOGENOMiHOG000083934.
InParanoidiP06710.
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.3 Publications

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

        10         20         30         40         50
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG
60 70 80 90 100
KTSIARLLAK GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK
110 120 130 140 150
VEDTRDLLDN VQYAPARGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEHV
160 170 180 190 200
KFLLATTDPQ KLPVTILSRC LQFHLKALDV EQIRHQLEHI LNEEHIAHEP
210 220 230 240 250
RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM LGTLDDDQAL
260 270 280 290 300
SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA
310 320 330 340 350
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE
360 370 380 390 400
MTLLRALAFH PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA
410 420 430 440 450
PTVPLPETTS QVLAARQQLQ RVQGATKAKK SEPAAATRAR PVNNAALERL
460 470 480 490 500
ASVTDRVQAR PVPSALEKAP AKKEAYRWKA TTPVMQQKEV VATPKALKKA
510 520 530 540 550
LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA LNAWKEESDN
560 570 580 590 600
AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL
610 620 630 640
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI

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.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei431 – 4311S → E in isoform gamma. CuratedVSP_042848
Alternative sequencei432 – 643212Missing in isoform gamma. CuratedVSP_042849Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P06710.
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: November 26, 2014
This is version 151 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