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P10443

- DPO3A_ECOLI

UniProt

P10443 - DPO3A_ECOLI

Protein

DNA polymerase III subunit alpha

Gene

dnaE

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 148 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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. The alpha chain is the DNA polymerase.

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: EcoliWiki
    3. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: GOC

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10238-MONOMER.
    ECOL316407:JW0179-MONOMER.
    MetaCyc:EG10238-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase III subunit alpha (EC:2.7.7.7)
    Gene namesi
    Name:dnaE
    Synonyms:polC
    Ordered Locus Names:b0184, JW0179
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10238. dnaE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. DNA polymerase III, core complex Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11601160DNA polymerase III subunit alphaPRO_0000103321Add
    BLAST

    Proteomic databases

    PaxDbiP10443.
    PRIDEiP10443.

    Expressioni

    Gene expression databases

    GenevestigatoriP10443.

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaNP0A98817EBI-549111,EBI-542385
    dnaQP0300720EBI-549111,EBI-549131
    dnaXP0671010EBI-549111,EBI-549140
    holAP286304EBI-549111,EBI-549153

    Protein-protein interaction databases

    DIPiDIP-9458N.
    IntActiP10443. 69 interactions.
    MINTiMINT-1224103.
    STRINGi511145.b0184.

    Structurei

    Secondary structure

    1
    1160
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni14 – 174
    Beta strandi18 – 203
    Helixi25 – 339
    Beta strandi37 – 448
    Helixi50 – 5910
    Beta strandi63 – 7311
    Helixi75 – 773
    Beta strandi82 – 887
    Helixi91 – 10616
    Helixi120 – 1245
    Beta strandi128 – 1314
    Helixi134 – 1363
    Helixi138 – 1458
    Helixi148 – 16114
    Beta strandi166 – 1705
    Helixi178 – 19215
    Beta strandi196 – 1983
    Beta strandi204 – 2063
    Helixi207 – 2093
    Helixi210 – 22112
    Helixi243 – 2497
    Turni250 – 2523
    Helixi254 – 26613
    Beta strandi284 – 2863
    Helixi288 – 30720
    Helixi311 – 3177
    Helixi319 – 33416
    Helixi338 – 35316
    Helixi365 – 3673
    Helixi369 – 3735
    Turni381 – 3855
    Helixi388 – 3903
    Beta strandi405 – 4073
    Helixi408 – 4103
    Helixi411 – 42212
    Helixi424 – 4263
    Beta strandi427 – 4304
    Beta strandi433 – 4353
    Helixi438 – 44811
    Helixi453 – 4608
    Helixi471 – 4777
    Helixi480 – 4878
    Helixi489 – 50113
    Beta strandi505 – 5084
    Beta strandi514 – 5174
    Helixi522 – 5243
    Beta strandi538 – 5414
    Helixi543 – 5486
    Beta strandi552 – 5565
    Helixi561 – 57414
    Turni575 – 5806
    Helixi586 – 5883
    Helixi594 – 6018
    Beta strandi608 – 6103
    Helixi614 – 62310
    Helixi628 – 63710
    Helixi640 – 6434
    Helixi647 – 6559
    Beta strandi657 – 6593
    Beta strandi666 – 6694
    Helixi671 – 6733
    Helixi674 – 6774
    Helixi678 – 6803
    Helixi687 – 69812
    Helixi702 – 71413
    Helixi717 – 73317
    Helixi738 – 75215
    Helixi758 – 77720
    Helixi779 – 78911
    Turni790 – 7923
    Helixi794 – 80613
    Turni816 – 8183
    Beta strandi820 – 8223
    Helixi835 – 8373
    Helixi843 – 85412
    Beta strandi855 – 8573
    Helixi862 – 8654
    Beta strandi871 – 8744
    Helixi876 – 8849
    Turni885 – 8917
    Helixi895 – 8995
    Beta strandi902 – 9054
    Helixi906 – 9094

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HNHX-ray2.30A1-910[»]
    2HQAX-ray2.60A1-917[»]
    4GX8X-ray1.70A/B/C/D1-270[»]
    4GX9X-ray2.15A/B/C/D1-270[»]
    4JOMX-ray2.90A1-917[»]
    ProteinModelPortaliP10443.
    SMRiP10443. Positions 1-910.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10443.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0587.
    HOGENOMiHOG000021784.
    KOiK02337.
    OMAiFCMDGRD.
    OrthoDBiEOG6CZQGR.
    PhylomeDBiP10443.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR011708. DNA_pol3_alpha.
    IPR029460. DNAPol_HHH.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    IPR004013. PHP_C.
    IPR003141. Pol/His_phosphatase_N.
    IPR016195. Pol/histidinol_Pase-like.
    IPR004805. PolC_alpha.
    [Graphical view]
    PfamiPF07733. DNA_pol3_alpha. 1 hit.
    PF14579. HHH_6. 1 hit.
    PF02811. PHP. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    SMARTiSM00481. POLIIIAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF89550. SSF89550. 1 hit.
    TIGRFAMsiTIGR00594. polc. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P10443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL     50
    VKFYGAGHGA GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL 100
    ISKAYQRGYG AAGPIIDRDW LIELNEGLIL LSGGRMGDVG RSLLRGNSAL 150
    VDECVAFYEE HFPDRYFLEL IRTGRPDEES YLHAAVELAE ARGLPVVATN 200
    DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM RSEEEMCELF 250
    ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL 300
    EERLAFLFPD EEERLKRRPE YDERLETELQ VINQMGFPGY FLIVMEFIQW 350
    SKDNGVPVGP GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP 400
    DFDVDFCMEK RDQVIEHVAD MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG 450
    HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ LPEIYEADEE VKALIDMARK 500
    LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ FDKSDVEYAG 550
    LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML 600
    QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN 650
    FIDRKHGREE ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY 700
    TLGGADMLRR AMGKKKPEEM AKQRSVFAEG AEKNGINAEL AMKIFDLVEK 750
    FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA EFMAAVMTAD MDNTEKVVGL 800
    VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG VGEGPIEAII 850
    EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN 900
    SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL 950
    DGERETLGLY LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVITAAGLV 1000
    VAARVMVTKR GNRIGICTLD DRSGRLEVML FTDALDKYQQ LLEKDRILIV 1050
    SGQVSFDDFS GGLKMTAREV MDIDEAREKY ARGLAISLTD RQIDDQLLNR 1100
    LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD RLLNDLRGLI 1150
    GSEQVELEFD 1160
    Length:1,160
    Mass (Da):129,905
    Last modified:July 1, 1989 - v1
    Checksum:i1A4F75F373841716
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19334 Genomic DNA. Translation: AAC36920.1.
    U70214 Genomic DNA. Translation: AAB08613.1.
    U00096 Genomic DNA. Translation: AAC73295.1.
    AP009048 Genomic DNA. Translation: BAA77859.1.
    S52931 mRNA. Translation: AAB24889.1.
    M96394 Genomic DNA. Translation: AAA70369.1. Sequence problems.
    D49445 Genomic DNA. Translation: BAA08424.1.
    PIRiC28390. DJEC3A.
    RefSeqiNP_414726.1. NC_000913.3.
    YP_488486.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73295; AAC73295; b0184.
    BAA77859; BAA77859; BAA77859.
    GeneIDi12933234.
    944877.
    KEGGiecj:Y75_p0180.
    eco:b0184.
    PATRICi32115479. VBIEscCol129921_0191.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19334 Genomic DNA. Translation: AAC36920.1 .
    U70214 Genomic DNA. Translation: AAB08613.1 .
    U00096 Genomic DNA. Translation: AAC73295.1 .
    AP009048 Genomic DNA. Translation: BAA77859.1 .
    S52931 mRNA. Translation: AAB24889.1 .
    M96394 Genomic DNA. Translation: AAA70369.1 . Sequence problems.
    D49445 Genomic DNA. Translation: BAA08424.1 .
    PIRi C28390. DJEC3A.
    RefSeqi NP_414726.1. NC_000913.3.
    YP_488486.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HNH X-ray 2.30 A 1-910 [» ]
    2HQA X-ray 2.60 A 1-917 [» ]
    4GX8 X-ray 1.70 A/B/C/D 1-270 [» ]
    4GX9 X-ray 2.15 A/B/C/D 1-270 [» ]
    4JOM X-ray 2.90 A 1-917 [» ]
    ProteinModelPortali P10443.
    SMRi P10443. Positions 1-910.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9458N.
    IntActi P10443. 69 interactions.
    MINTi MINT-1224103.
    STRINGi 511145.b0184.

    Chemistry

    BindingDBi P10443.
    ChEMBLi CHEMBL4621.

    Proteomic databases

    PaxDbi P10443.
    PRIDEi P10443.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73295 ; AAC73295 ; b0184 .
    BAA77859 ; BAA77859 ; BAA77859 .
    GeneIDi 12933234.
    944877.
    KEGGi ecj:Y75_p0180.
    eco:b0184.
    PATRICi 32115479. VBIEscCol129921_0191.

    Organism-specific databases

    EchoBASEi EB0234.
    EcoGenei EG10238. dnaE.

    Phylogenomic databases

    eggNOGi COG0587.
    HOGENOMi HOG000021784.
    KOi K02337.
    OMAi FCMDGRD.
    OrthoDBi EOG6CZQGR.
    PhylomeDBi P10443.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10238-MONOMER.
    ECOL316407:JW0179-MONOMER.
    MetaCyc:EG10238-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10443.
    PROi P10443.

    Gene expression databases

    Genevestigatori P10443.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR011708. DNA_pol3_alpha.
    IPR029460. DNAPol_HHH.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    IPR004013. PHP_C.
    IPR003141. Pol/His_phosphatase_N.
    IPR016195. Pol/histidinol_Pase-like.
    IPR004805. PolC_alpha.
    [Graphical view ]
    Pfami PF07733. DNA_pol3_alpha. 1 hit.
    PF14579. HHH_6. 1 hit.
    PF02811. PHP. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    SMARTi SM00481. POLIIIAc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89550. SSF89550. 1 hit.
    TIGRFAMsi TIGR00594. polc. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the Escherichia coli dnaE gene."
      Tomasiewicz H.G., McHenry C.S.
      J. Bacteriol. 169:5735-5744(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Tomasiewicz H.G., McHenry C.S.
      J. Bacteriol. 173:4549-4549(1991) [PubMed] [Europe PMC] [Abstract]
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "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.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis."
      Li S.-J., Cronan J.E. Jr.
      J. Bacteriol. 175:332-340(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1070-1160.
    8. Yamamoto Y.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1137-1160.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "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.
    10. "Antimutator mutations in the alpha subunit of Escherichia coli DNA polymerase III: identification of the responsible mutations and alignment with other DNA polymerases."
      Fijalkowska I.J., Schaaper R.M.
      Genetics 134:1039-1044(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.

    Entry informationi

    Entry nameiDPO3A_ECOLI
    AccessioniPrimary (citable) accession number: P10443
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 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, 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