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P06710

- DPO3X_ECOLI

UniProt

P06710 - DPO3X_ECOLI

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
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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
    8. protein binding Source: IntAct

    GO - Biological processi

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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06710.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DnaX/STICHEL family.Curated

    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.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

    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. CuratedVSP_042848
    Alternative sequencei432 – 643212Missing in isoform gamma. CuratedVSP_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

    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: October 1, 2014
    This is version 149 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