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Protein

DNA polymerase III subunit alpha

Gene

dnaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria (PubMed:2932432). This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit (PubMed:2932432). It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius (PubMed:2413035).2 Publications

Catalytic activityi

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

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA-directed DNA polymerase activity Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
Biological processDNA replication

Enzyme and pathway databases

BioCyciEcoCyc:EG10238-MONOMER
MetaCyc:EG10238-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit alpha (EC:2.7.7.71 Publication)
Gene namesi
Name:dnaE
Synonyms:polC
Ordered Locus Names:b0184, JW0179
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10238 dnaE

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi920 – 924QADMF → PADMP: Loss of interaction with beta sliding clamp (dnaN). 1 Publication5
Mutagenesisi921 – 923ADM → LDL: Increases binding to beta sliding clamp (dnaN), increases stability of enzyme complex. 1 Publication3
Mutagenesisi923 – 924MF → KK: Loss of interaction with beta sliding clamp (dnaN). 1 Publication2

Chemistry databases

ChEMBLiCHEMBL4621

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001033211 – 1160DNA polymerase III subunit alphaAdd BLAST1160

Proteomic databases

PaxDbiP10443
PRIDEiP10443

Interactioni

Subunit structurei

The DNA polymerase III holoenzyme complex contains at least 10 different subunits 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 (PubMed:2040637). The polymerase is tethered to the template via the dimeric beta sliding clamp processivity factor. The clamp loader (also called gamma complex) assembles the beta sliding clamp onto the primed template and plays a central role in the organization and communication at the replication fork. The clamp-loading complex contains delta, delta', psi and chi, and 3 copies of either or both of two different DnaX proteins, gamma and tau. The DNA replisome complex has a single clamp loader (3 tau and 1 each of delta, delta', psi and chi subunits) which binds 3 Pol III cores (1 core on the leading strand and 2 on the lagging strand) each with a beta sliding clamp dimer. Additional proteins in the replisome are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase (PubMed:20413500, PubMed:22157955). Interacts with the beta sliding-clamp subunit via the peptide Gln-Ala-Asp-Met-Phe (residues 920-924) (PubMed:11573000).4 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4262228, 218 interactors
ComplexPortaliCPX-1925 DNA polymerase III proofreading complex
DIPiDIP-9458N
IntActiP10443, 70 interactors
MINTiP10443
STRINGi316385.ECDH10B_0164

Chemistry databases

BindingDBiP10443

Structurei

Secondary structure

11160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP10443
SMRiP10443
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10443

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C0B Bacteria
COG0587 LUCA
HOGENOMiHOG000021784
InParanoidiP10443
KOiK02337
PhylomeDBiP10443

Family and domain databases

InterProiView protein in InterPro
IPR011708 DNA_pol3_alpha
IPR029460 DNAPol_HHH
IPR004365 NA-bd_OB_tRNA
IPR004013 PHP_dom
IPR003141 Pol/His_phosphatase_N
IPR016195 Pol/histidinol_Pase-like
IPR004805 PolC_alpha
PANTHERiPTHR32294 PTHR32294, 1 hit
PfamiView protein in Pfam
PF07733 DNA_pol3_alpha, 1 hit
PF14579 HHH_6, 1 hit
PF02811 PHP, 1 hit
PF01336 tRNA_anti-codon, 1 hit
SMARTiView protein in SMART
SM00481 POLIIIAc, 1 hit
SUPFAMiSSF89550 SSF89550, 1 hit
TIGRFAMsiTIGR00594 polc, 1 hit

Sequencei

Sequence statusi: Complete.

P10443-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL
60 70 80 90 100
VKFYGAGHGA GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL
110 120 130 140 150
ISKAYQRGYG AAGPIIDRDW LIELNEGLIL LSGGRMGDVG RSLLRGNSAL
160 170 180 190 200
VDECVAFYEE HFPDRYFLEL IRTGRPDEES YLHAAVELAE ARGLPVVATN
210 220 230 240 250
DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM RSEEEMCELF
260 270 280 290 300
ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL
310 320 330 340 350
EERLAFLFPD EEERLKRRPE YDERLETELQ VINQMGFPGY FLIVMEFIQW
360 370 380 390 400
SKDNGVPVGP GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP
410 420 430 440 450
DFDVDFCMEK RDQVIEHVAD MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG
460 470 480 490 500
HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ LPEIYEADEE VKALIDMARK
510 520 530 540 550
LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ FDKSDVEYAG
560 570 580 590 600
LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML
610 620 630 640 650
QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN
660 670 680 690 700
FIDRKHGREE ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY
710 720 730 740 750
TLGGADMLRR AMGKKKPEEM AKQRSVFAEG AEKNGINAEL AMKIFDLVEK
760 770 780 790 800
FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA EFMAAVMTAD MDNTEKVVGL
810 820 830 840 850
VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG VGEGPIEAII
860 870 880 890 900
EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN
910 920 930 940 950
SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL
960 970 980 990 1000
DGERETLGLY LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVITAAGLV
1010 1020 1030 1040 1050
VAARVMVTKR GNRIGICTLD DRSGRLEVML FTDALDKYQQ LLEKDRILIV
1060 1070 1080 1090 1100
SGQVSFDDFS GGLKMTAREV MDIDEAREKY ARGLAISLTD RQIDDQLLNR
1110 1120 1130 1140 1150
LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD RLLNDLRGLI
1160
GSEQVELEFD
Length:1,160
Mass (Da):129,905
Last modified:July 1, 1989 - v1
Checksum:i1A4F75F373841716
GO

Sequence cautioni

The sequence AAA70369 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 Different initiation.
D49445 Genomic DNA Translation: BAA08424.1
PIRiC28390 DJEC3A
RefSeqiNP_414726.1, NC_000913.3
WP_001294757.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73295; AAC73295; b0184
BAA77859; BAA77859; BAA77859
GeneIDi944877
KEGGiecj:JW0179
eco:b0184
PATRICifig|1411691.4.peg.2095

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 Different initiation.
D49445 Genomic DNA Translation: BAA08424.1
PIRiC28390 DJEC3A
RefSeqiNP_414726.1, NC_000913.3
WP_001294757.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FKUelectron microscopy8.34A1-1160[»]
5FKVelectron microscopy8.00A1-1160[»]
5FKWelectron microscopy7.30A1-1160[»]
5M1Selectron microscopy6.70A1-927[»]
ProteinModelPortaliP10443
SMRiP10443
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262228, 218 interactors
ComplexPortaliCPX-1925 DNA polymerase III proofreading complex
DIPiDIP-9458N
IntActiP10443, 70 interactors
MINTiP10443
STRINGi316385.ECDH10B_0164

Chemistry databases

BindingDBiP10443
ChEMBLiCHEMBL4621

Proteomic databases

PaxDbiP10443
PRIDEiP10443

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73295; AAC73295; b0184
BAA77859; BAA77859; BAA77859
GeneIDi944877
KEGGiecj:JW0179
eco:b0184
PATRICifig|1411691.4.peg.2095

Organism-specific databases

EchoBASEiEB0234
EcoGeneiEG10238 dnaE

Phylogenomic databases

eggNOGiENOG4105C0B Bacteria
COG0587 LUCA
HOGENOMiHOG000021784
InParanoidiP10443
KOiK02337
PhylomeDBiP10443

Enzyme and pathway databases

BioCyciEcoCyc:EG10238-MONOMER
MetaCyc:EG10238-MONOMER

Miscellaneous databases

EvolutionaryTraceiP10443
PROiPR:P10443

Family and domain databases

InterProiView protein in InterPro
IPR011708 DNA_pol3_alpha
IPR029460 DNAPol_HHH
IPR004365 NA-bd_OB_tRNA
IPR004013 PHP_dom
IPR003141 Pol/His_phosphatase_N
IPR016195 Pol/histidinol_Pase-like
IPR004805 PolC_alpha
PANTHERiPTHR32294 PTHR32294, 1 hit
PfamiView protein in Pfam
PF07733 DNA_pol3_alpha, 1 hit
PF14579 HHH_6, 1 hit
PF02811 PHP, 1 hit
PF01336 tRNA_anti-codon, 1 hit
SMARTiView protein in SMART
SM00481 POLIIIAc, 1 hit
SUPFAMiSSF89550 SSF89550, 1 hit
TIGRFAMsiTIGR00594 polc, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDPO3A_ECOLI
AccessioniPrimary (citable) accession number: P10443
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 7, 2018
This is version 177 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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