Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase III subunit theta

Gene

holE

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. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
The exact function of the theta subunit is unknown.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG11505-MONOMER
MetaCyc:EG11505-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit theta (EC:2.7.7.7)
Gene namesi
Name:holE
Ordered Locus Names:b1842, JW1831
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11505 holE

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • DNA polymerase III, core complex Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001055221 – 76DNA polymerase III subunit thetaAdd BLAST76

Proteomic databases

PaxDbiP0ABS8
PRIDEiP0ABS8

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
dnaQP0300713EBI-549182,EBI-549131

Protein-protein interaction databases

BioGridi4260361, 41 interactors
DIPiDIP-39982N
IntActiP0ABS8, 29 interactors
MINTiP0ABS8
STRINGi316385.ECDH10B_1983

Structurei

Secondary structure

176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Helixi11 – 21Combined sources11
Beta strandi23 – 25Combined sources3
Helixi27 – 30Combined sources4
Helixi38 – 43Combined sources6
Helixi47 – 53Combined sources7
Helixi54 – 56Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi67 – 69Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DU2NMR-A1-76[»]
2AE9NMR-A1-76[»]
2AXDNMR-S1-76[»]
2XY8NMR-B1-76[»]
5M1Selectron microscopy6.70F10-65[»]
ProteinModelPortaliP0ABS8
SMRiP0ABS8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABS8

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105MPK Bacteria
ENOG4111UZC LUCA
HOGENOMiHOG000219272
KOiK02345
OMAiFRERYNM

Family and domain databases

Gene3Di1.20.58.250, 1 hit
InterProiView protein in InterPro
IPR009052 DNA_pol_III_theta_bac
IPR036745 PolIII_theta_sf
PfamiView protein in Pfam
PF06440 DNA_pol3_theta, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD057609 DNA_pol_III_theta_bac, 1 hit

Sequencei

Sequence statusi: Complete.

P0ABS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKNLAKLDQ TEMDKVNVDL AAAGVAFKER YNMPVIAEAV EREQPEHLRS
60 70
WFRERLIAHR LASVNLSRLP YEPKLK
Length:76
Mass (Da):8,846
Last modified:October 25, 2005 - v1
Checksum:i3667D87327E96556
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04572 Genomic DNA Translation: AAA23697.1
L05381 Genomic DNA Translation: AAA23982.1
U00096 Genomic DNA Translation: AAC74912.1
AP009048 Genomic DNA Translation: BAA15650.1
PIRiS34951
RefSeqiNP_416356.1, NC_000913.3
WP_000916763.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74912; AAC74912; b1842
BAA15650; BAA15650; BAA15650
GeneIDi947471
KEGGiecj:JW1831
eco:b1842
PATRICifig|511145.12.peg.1920

Similar proteinsi

Entry informationi

Entry nameiHOLE_ECOLI
AccessioniPrimary (citable) accession number: P0ABS8
Secondary accession number(s): P28689
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: March 28, 2018
This is version 93 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, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health