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 delta'

Gene

holB

Organism
Yersinia pestis
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 (By similarity).By similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit delta' (EC:2.7.7.7)
Gene namesi
Name:holB
Ordered Locus Names:YPO1606, y1765, YP_2248
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000815 Componenti: Chromosome
  • UP000001019 Componenti: Chromosome
  • UP000002490 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001055161 – 340DNA polymerase III subunit delta'Add BLAST340

Proteomic databases

PaxDbiO69170

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] (By similarity).By similarity

Protein-protein interaction databases

STRINGi187410.y1765

Structurei

3D structure databases

ProteinModelPortaliO69170
SMRiO69170
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4107QRG Bacteria
COG0470 LUCA
HOGENOMiHOG000192595
KOiK02341
OMAiQRGHAWL

Family and domain databases

InterProiView protein in InterPro
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR004622 DNA_pol_HolB
IPR015199 DNA_pol_III_delta_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF09115 DNApol3-delta_C, 1 hit
SUPFAMiSSF48019 SSF48019, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00678 holB, 1 hit

Sequencei

Sequence statusi: Complete.

O69170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNWYPWLNAP YRQLVGQHST GRGHHALLLH SLPGNGEDAL IYALSRWLMC
60 70 80 90 100
QQRQGEKSCG ECHSCRLMLA GNHPDWYVLT PEKGKSSIGV ELVRQLIDKL
110 120 130 140 150
YSHAQQGGAK VVWLPHAEVL TDAAANALLK TLEEPPEKTY FLLDCHQPAS
160 170 180 190 200
LLATLRSRCF YWYLACPDTA ICLQWLNLQW RKRQIPVEPV AMLAALKLSE
210 220 230 240 250
GAPLAAERLL QPERWSIRSA LCSGLREALN RSDLLSLLPQ LNHDDAAERL
260 270 280 290 300
QWLSSLLLDA LKWQQGAGEF AVNQDQLPLV QQLAHIAATP VLLQLAKQLA
310 320 330 340
HCRHQLLSVV GVNRELLLTE QLLSWETALS TGTYSTLPSL
Length:340
Mass (Da):38,114
Last modified:November 16, 2001 - v2
Checksum:iC4F199180586C6C9
GO

Sequence cautioni

The sequence AAM85333 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAS62454 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti137E → Q in AAC18856 (PubMed:10491164).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA Translation: CAL20251.1
AE009952 Genomic DNA Translation: AAM85333.1 Different initiation.
AE017042 Genomic DNA Translation: AAS62454.1 Different initiation.
AF065312 Genomic DNA Translation: AAC18856.1
PIRiAI0195
RefSeqiWP_002213083.1, NZ_PDBR01000114.1
YP_002346617.1, NC_003143.1

Genome annotation databases

EnsemblBacteriaiAAM85333; AAM85333; y1765
AAS62454; AAS62454; YP_2248
GeneIDi1174445
KEGGiype:YPO1606
ypk:y1765
ypm:YP_2248
PATRICifig|214092.21.peg.1949

Similar proteinsi

Entry informationi

Entry nameiHOLB_YERPE
AccessioniPrimary (citable) accession number: O69170
Secondary accession number(s): Q0WGH1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 16, 2001
Last modified: March 28, 2018
This is version 122 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health