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P10443 (DPO3A_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase III subunit alpha
EC=2.7.7.7
Gene names
Name:dnaE
Synonyms:polC
Ordered Locus Names:b0184, JW0179
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length1160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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].

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the DNA polymerase type-C family. DnaE subfamily.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3'-5' exonuclease activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed DNA polymerase activity

Inferred from direct assay. Source: EcoliWiki

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dnaQP030078EBI-549111,EBI-549131

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11601160DNA polymerase III subunit alpha
PRO_0000103321

Secondary structure

1 ................................................................................................................................................. 1160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10443 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 1A4F75F373841716

FASTA1,160129,905
        10         20         30         40         50         60 
MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL VKFYGAGHGA 

        70         80         90        100        110        120 
GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL ISKAYQRGYG AAGPIIDRDW 

       130        140        150        160        170        180 
LIELNEGLIL LSGGRMGDVG RSLLRGNSAL VDECVAFYEE HFPDRYFLEL IRTGRPDEES 

       190        200        210        220        230        240 
YLHAAVELAE ARGLPVVATN DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM 

       250        260        270        280        290        300 
RSEEEMCELF ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL 

       310        320        330        340        350        360 
EERLAFLFPD EEERLKRRPE YDERLETELQ VINQMGFPGY FLIVMEFIQW SKDNGVPVGP 

       370        380        390        400        410        420 
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIEHVAD 

       430        440        450        460        470        480 
MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ 

       490        500        510        520        530        540 
LPEIYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ 

       550        560        570        580        590        600 
FDKSDVEYAG LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML 

       610        620        630        640        650        660 
QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE 

       670        680        690        700        710        720 
ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM 

       730        740        750        760        770        780 
AKQRSVFAEG AEKNGINAEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA 

       790        800        810        820        830        840 
EFMAAVMTAD MDNTEKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG 

       850        860        870        880        890        900 
VGEGPIEAII EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN 

       910        920        930        940        950        960 
SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL DGERETLGLY 

       970        980        990       1000       1010       1020 
LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVITAAGLV VAARVMVTKR GNRIGICTLD 

      1030       1040       1050       1060       1070       1080 
DRSGRLEVML FTDALDKYQQ LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY 

      1090       1100       1110       1120       1130       1140 
ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD 

      1150       1160 
RLLNDLRGLI GSEQVELEFD

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Escherichia coli dnaE gene."
Tomasiewicz H.G., McHenry C.S.
J. Bacteriol. 169:5735-5744(1987) [PubMed: 3316192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Tomasiewicz H.G., McHenry C.S.
J. Bacteriol. 173:4549-4549(1991) [PubMed: 2066347] [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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 7678242] [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: 1575709] [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: 8375647] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRDJEC3A. C28390.
RefSeqNP_414726.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HNHX-ray2.30A1-910[»]
2HQAX-ray2.60A1-917[»]
ProteinModelPortalP10443.
SMRP10443. Positions 1-910.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9458N.
IntActP10443. 67 interactions.
MINTMINT-1224103.

Proteomic databases

PRIDEP10443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003957; EBESCP00000003957; EBESCG00000003242.
EBESCT00000015810; EBESCP00000015101; EBESCG00000014870.
GeneID944877.
GenomeReviewsGene locus JW0179 in contig AP009048_GR.
Gene locus b0184 in contig U00096_GR.
KEGGecj:JW0179.
eco:b0184.
PATRIC32115479. VBIEscCol129921_0191.

Organism-specific databases

EchoBASEEB0234.
EcoGeneEG10238. dnaE.

Phylogenomic databases

eggNOGCOG0587.
GeneTreeEBGT00050000010406.
HOGENOMHBG734490.
OMARVLQMPY.
PhylomeDBP10443.
ProtClustDBPRK05673.

Enzyme and pathway databases

BioCycEcoCyc:EG10238-MONOMER.
MetaCyc:EG10238-MONOMER.

Gene expression databases

GenevestigatorP10443.

Family and domain databases

InterProIPR011708. DNA_pol3_alpha.
IPR004365. NA-bd_OB_tRNA-helicase.
IPR004013. PHP_C.
IPR003141. Pol/His_phosphatase_N.
IPR016195. Pol/histidinol_Pase-like.
IPR004805. PolC_alpha.
[Graphical view]
KOK02337.
PfamPF07733. DNA_pol3_alpha. 1 hit.
PF02811. PHP. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
SMARTSM00481. POLIIIAc. 1 hit.
[Graphical view]
SUPFAMSSF89550. PHP-like. 1 hit.
TIGRFAMsTIGR00594. Polc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPO3A_ECOLI
AccessionPrimary (citable) accession number: P10443
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 25, 2012
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents