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Protein

DNA polymerase III subunit chi

Gene

holC

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

Functioni

Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex (PubMed:2040637). 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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • DNA replication Source: UniProtKB-KW
  • positive regulation of DNA-dependent DNA replication initiation Source: EcoliWiki
  • response to radiation Source: EcoCyc

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG11413-MONOMER
MetaCyc:EG11413-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit chi (EC:2.7.7.7)
Gene namesi
Name:holC
Ordered Locus Names:b4259, JW4216
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11413 holC

Subcellular locationi

GO - Cellular componenti

  • DNA polymerase III, clamp loader chi/psi subcomplex Source: EcoliWiki

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001055171 – 147DNA polymerase III subunit chiAdd BLAST147

Proteomic databases

PaxDbiP28905
PRIDEiP28905

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-loading complex (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). The clamp loader hydrolyzes ATP to assemble the beta processivity factor onto the primed template (PubMed:2040637) and plays a central role in the organization and communication at the replication fork.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4262725, 159 interactors
DIPiDIP-9933N
IntActiP28905, 41 interactors
MINTiP28905
STRINGi316385.ECDH10B_4452

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi20 – 34Combined sources15
Beta strandi39 – 42Combined sources4
Helixi46 – 55Combined sources10
Turni56 – 58Combined sources3
Beta strandi67 – 69Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi94 – 98Combined sources5
Helixi105 – 109Combined sources5
Beta strandi111 – 117Combined sources7
Helixi121 – 123Combined sources3
Helixi124 – 136Combined sources13
Beta strandi140 – 144Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EM8X-ray2.10A/C1-147[»]
3SXUX-ray1.85A1-147[»]
ProteinModelPortaliP28905
SMRiP28905
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28905

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105MYG Bacteria
COG2927 LUCA
HOGENOMiHOG000263567
InParanoidiP28905
KOiK02339
OMAiPVELCWP

Family and domain databases

Gene3Di3.40.50.10110, 1 hit
InterProiView protein in InterPro
IPR007459 DNA_pol3_chi
IPR036768 PolIII_chi_sf
PANTHERiPTHR38767 PTHR38767, 1 hit
PfamiView protein in Pfam
PF04364 DNA_pol3_chi, 1 hit
SUPFAMiSSF102400 SSF102400, 1 hit

Sequencei

Sequence statusi: Complete.

P28905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNATFYLLD NDTTVDGLSA VEQLVCEIAA ERWRSGKRVL IACEDEKQAY
60 70 80 90 100
RLDEALWARP AESFVPHNLA GEGPRGGAPV EIAWPQKRSS SRRDILISLR
110 120 130 140
TSFADFATAF TEVVDFVPYE DSLKQLARER YKAYRVAGFN LNTATWK
Length:147
Mass (Da):16,633
Last modified:December 1, 1992 - v1
Checksum:i7FEFFC359B28AA88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04574 Genomic DNA Translation: AAA70368.1
Z14155 Genomic DNA Translation: CAA78524.1
U14003 Genomic DNA Translation: AAA97156.1
U00096 Genomic DNA Translation: AAC77216.1
AP009048 Genomic DNA Translation: BAE78256.1
X15130 Genomic DNA Translation: CAA33226.1
PIRiA46739
RefSeqiNP_418680.1, NC_000913.3
WP_000786400.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77216; AAC77216; b4259
BAE78256; BAE78256; BAE78256
GeneIDi948787
KEGGiecj:JW4216
eco:b4259
PATRICifig|1411691.4.peg.2445

Similar proteinsi

Entry informationi

Entry nameiHOLC_ECOLI
AccessioniPrimary (citable) accession number: P28905
Secondary accession number(s): P11649, Q2M650
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: March 28, 2018
This is version 137 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
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Main funding by: National Institutes of Health