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P10443

- DPO3A_ECOLI

UniProt

P10443 - DPO3A_ECOLI

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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

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

GO - Biological processi

  1. DNA-dependent DNA replication Source: GOC
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP10443.
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

        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 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.
InParanoidi P10443.
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

« Hide 'large scale' publications
  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 29, 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, 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