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
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • DNA-dependent DNA replication Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

BioCyciEcoCyc:EG11500-MONOMER.
ECOL316407:JW1085-MONOMER.
MetaCyc:EG11500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit delta' (EC:2.7.7.7)
Gene namesi
Name:holB
Ordered Locus Names:b1099, JW1085
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11500. holB.

Subcellular locationi

GO - Cellular componenti

  • DNA polymerase III complex Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001055131 – 334DNA polymerase III subunit delta'Add BLAST334

Proteomic databases

PaxDbiP28631.
PRIDEiP28631.

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
dnaXP0671017EBI-549161,EBI-549140
dnaXP06710-16EBI-549161,EBI-6464728
holAP2863017EBI-549161,EBI-549153
holCP289055EBI-549161,EBI-549169
mutLP233672EBI-549161,EBI-554913

Protein-protein interaction databases

BioGridi4263116. 175 interactors.
DIPiDIP-9932N.
IntActiP28631. 25 interactors.
MINTiMINT-1239429.
STRINGi511145.b1099.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi8 – 19Combined sources12
Beta strandi25 – 30Combined sources6
Helixi37 – 48Combined sources12
Beta strandi55 – 57Combined sources3
Helixi63 – 70Combined sources8
Beta strandi76 – 79Combined sources4
Beta strandi86 – 88Combined sources3
Helixi90 – 99Combined sources10
Beta strandi110 – 115Combined sources6
Helixi117 – 119Combined sources3
Helixi122 – 132Combined sources11
Beta strandi139 – 146Combined sources8
Helixi148 – 150Combined sources3
Helixi153 – 156Combined sources4
Beta strandi159 – 163Combined sources5
Helixi169 – 179Combined sources11
Helixi184 – 193Combined sources10
Turni194 – 196Combined sources3
Helixi198 – 203Combined sources6
Helixi208 – 226Combined sources19
Helixi230 – 232Combined sources3
Helixi233 – 236Combined sources4
Helixi241 – 255Combined sources15
Turni259 – 261Combined sources3
Helixi271 – 280Combined sources10
Helixi283 – 303Combined sources21
Helixi308 – 322Combined sources15
Beta strandi324 – 326Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5TX-ray2.20A1-334[»]
1JR3X-ray2.70E1-334[»]
1XXHX-ray3.45E/J1-334[»]
1XXIX-ray4.10E/J1-334[»]
3GLFX-ray3.39E/J1-334[»]
3GLGX-ray3.25E/J1-334[»]
3GLHX-ray3.89E/J/O1-334[»]
3GLIX-ray3.50E/J1-334[»]
ProteinModelPortaliP28631.
SMRiP28631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28631.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4107QRG. Bacteria.
COG0470. LUCA.
HOGENOMiHOG000192595.
InParanoidiP28631.
KOiK02341.
OMAiCHSCHLM.
PhylomeDBiP28631.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008921. DNA_pol3_clamp-load_cplx_C.
IPR004622. DNA_pol_HolB.
IPR015199. DNA_pol_III_delta_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF09115. DNApol3-delta_C. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00678. holB. 1 hit.

Sequencei

Sequence statusi: Complete.

P28631-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRWYPWLRPD FEKLVASYQA GRGHHALLIQ ALPGMGDDAL IYALSRYLLC
60 70 80 90 100
QQPQGHKSCG HCRGCQLMQA GTHPDYYTLA PEKGKNTLGV DAVREVTEKL
110 120 130 140 150
NEHARLGGAK VVWVTDAALL TDAAANALLK TLEEPPAETW FFLATREPER
160 170 180 190 200
LLATLRSRCR LHYLAPPPEQ YAVTWLSREV TMSQDALLAA LRLSAGSPGA
210 220 230 240 250
ALALFQGDNW QARETLCQAL AYSVPSGDWY SLLAALNHEQ APARLHWLAT
260 270 280 290 300
LLMDALKRHH GAAQVTNVDV PGLVAELANH LSPSRLQAIL GDVCHIREQL
310 320 330
MSVTGINREL LITDLLLRIE HYLQPGVVLP VPHL
Length:334
Mass (Da):36,937
Last modified:November 1, 1997 - v2
Checksum:iDC9DAA644AD8A096
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166P → G in AAA23708 (PubMed:8505303).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04577 Genomic DNA. Translation: AAA23708.1.
L01483 Genomic DNA. Translation: AAA23696.1.
U00096 Genomic DNA. Translation: AAC74183.1.
AP009048 Genomic DNA. Translation: BAA35906.1.
PIRiS35523.
RefSeqiNP_415617.1. NC_000913.3.
WP_001267956.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74183; AAC74183; b1099.
BAA35906; BAA35906; BAA35906.
GeneIDi945661.
KEGGiecj:JW1085.
eco:b1099.
PATRICi32117439. VBIEscCol129921_1142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04577 Genomic DNA. Translation: AAA23708.1.
L01483 Genomic DNA. Translation: AAA23696.1.
U00096 Genomic DNA. Translation: AAC74183.1.
AP009048 Genomic DNA. Translation: BAA35906.1.
PIRiS35523.
RefSeqiNP_415617.1. NC_000913.3.
WP_001267956.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5TX-ray2.20A1-334[»]
1JR3X-ray2.70E1-334[»]
1XXHX-ray3.45E/J1-334[»]
1XXIX-ray4.10E/J1-334[»]
3GLFX-ray3.39E/J1-334[»]
3GLGX-ray3.25E/J1-334[»]
3GLHX-ray3.89E/J/O1-334[»]
3GLIX-ray3.50E/J1-334[»]
ProteinModelPortaliP28631.
SMRiP28631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263116. 175 interactors.
DIPiDIP-9932N.
IntActiP28631. 25 interactors.
MINTiMINT-1239429.
STRINGi511145.b1099.

Proteomic databases

PaxDbiP28631.
PRIDEiP28631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74183; AAC74183; b1099.
BAA35906; BAA35906; BAA35906.
GeneIDi945661.
KEGGiecj:JW1085.
eco:b1099.
PATRICi32117439. VBIEscCol129921_1142.

Organism-specific databases

EchoBASEiEB1463.
EcoGeneiEG11500. holB.

Phylogenomic databases

eggNOGiENOG4107QRG. Bacteria.
COG0470. LUCA.
HOGENOMiHOG000192595.
InParanoidiP28631.
KOiK02341.
OMAiCHSCHLM.
PhylomeDBiP28631.

Enzyme and pathway databases

BioCyciEcoCyc:EG11500-MONOMER.
ECOL316407:JW1085-MONOMER.
MetaCyc:EG11500-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP28631.
PROiP28631.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008921. DNA_pol3_clamp-load_cplx_C.
IPR004622. DNA_pol_HolB.
IPR015199. DNA_pol_III_delta_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF09115. DNApol3-delta_C. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00678. holB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHOLB_ECOLI
AccessioniPrimary (citable) accession number: P28631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 151 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.