Skip Header

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

UniProtKB - P06710 (DPO3X_ECOLI)

Entry version 189 (16 Oct 2019)
Sequence version 1 (01 Jan 1988)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

DNA polymerase III subunit tau

Gene

dnaX

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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'-5' exonuclease activity. The gamma complex (gamma3,delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA (PubMed:9927437).1 Publication
Isoform tau: serves as a scaffold to trimerize the core complex (PubMed:7037770).1 Publication
Isoform gamma: interacts with the delta and delta' subunits to transfer the beta subunit on the DNA (PubMed:9927437). Interacts with ATP, drives ATP-induced conformational changes in the gamma complex that opens the beta sliding clamp ring. After loading of primed DNA ATP is hydrolyzed and the beta sliding clamp ring closes (PubMed:9927437).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi45 – 52ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

  • DNA-dependent DNA replication Source: GO_Central
  • DNA replication Source: EcoliWiki
Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		ECOL316407:JW0459-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA polymerase III subunit tau (EC:2.7.7.7)
Alternative name(s):
DNA polymerase III subunit gamma
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:dnaX
Synonyms:dnaZ, dnaZX
Ordered Locus Names:b0470, JW0459
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10245 dnaX

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Complete GO annotation on QuickGO ...

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi118G → D in dnaX2016(Ts); present in both isoforms, unable to grow at 42 degrees Celsius. 1 Publication1
Mutagenesisi601E → K in dnaX36(Ts); present only in isoform tau, unable to grow at 42 degrees Celsius. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02930 Adenosine 5'-[Gama-thio]triphosphate

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000073602 – 643DNA polymerase III subunit tauAdd BLAST642

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P06710

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06710

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06710

PRoteomics IDEntifications database

More...PRIDEi		P06710

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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, PubMed:9927437) and plays a central role in the organization and communication at the replication fork; the minimal complex to load the beta sliding clamp on DNA is delta, delta', gamma (PubMed:9927437).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259846, 140 interactors
849494, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1926 DNA polymerase III clamp loader complex [P06710-2]

Database of interacting proteins

More...DIPi		DIP-9464N

Protein interaction database and analysis system

More...IntActi		P06710, 33 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0470

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06710

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06710

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06710

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DnaX/STICHEL family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4107QMP Bacteria
COG2812 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000083934

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06710

KEGG Orthology (KO)

More...KOi		K02343

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06710

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.300.150, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593 AAA+_ATPase
IPR001270 ClpA/B
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR022001 DNA_pol3_tau_IV
IPR022754 DNA_pol_III_gamma-3
IPR012763 DNA_pol_III_sug/sutau
IPR021029 DNA_pol_III_tau_dom-5
IPR027417 P-loop_NTPase
IPR038249 PolIII_tau_C_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12169 DNA_pol3_gamma3, 1 hit
PF12168 DNA_pol3_tau_4, 1 hit
PF12170 DNA_pol3_tau_5, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00300 CLPPROTEASEA

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48019 SSF48019, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02397 dnaX_nterm, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Note: The production of the two protein products from this region is due to programmed ribosomal frameshifting. Frameshifting is about 40% efficient.3 Publications
Isoform tau (identifier: P06710-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG 
        60         70         80         90        100
KTSIARLLAK GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK 
       110        120        130        140        150
VEDTRDLLDN VQYAPARGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEHV 
       160        170        180        190        200
KFLLATTDPQ KLPVTILSRC LQFHLKALDV EQIRHQLEHI LNEEHIAHEP 
       210        220        230        240        250
RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM LGTLDDDQAL 
       260        270        280        290        300
SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA 
       310        320        330        340        350
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE 
       360        370        380        390        400
MTLLRALAFH PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA 
       410        420        430        440        450
PTVPLPETTS QVLAARQQLQ RVQGATKAKK SEPAAATRAR PVNNAALERL 
       460        470        480        490        500
ASVTDRVQAR PVPSALEKAP AKKEAYRWKA TTPVMQQKEV VATPKALKKA 
       510        520        530        540        550
LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA LNAWKEESDN 
       560        570        580        590        600
AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL 
       610        620        630        640 
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI
Note: Produced by full-length translation of the dnaX gene. This isoform is essential, constructs that express only the gamma isoform are not viable (PubMed:8376347).1 Publication
Length:643
Mass (Da):71,138
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD2028BD99E375150
GO
Isoform gamma (identifier: P06710-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     431-431: S → E
     432-643: Missing.

Note: Formed by programmed ribosomal frameshifting to a premature stop codon in the -1 frame at codon 430, the last residue is thus Glu and not Ser. Mutants which remove the frameshift are viable, suggesting strongly that gamma is not essential for viability (PubMed:8376347).4 Publications
Show »
Length:431
Mass (Da):47,545
Checksum:i8177A07F31BC86E3
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA28175 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042848431S → E in isoform gamma. Curated1
Alternative sequenceiVSP_042849432 – 643Missing in isoform gamma. CuratedAdd BLAST212

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X04487 Genomic DNA Translation: CAA28174.1
X04487 Genomic DNA Translation: CAA28175.1 Different initiation.
X04275 Genomic DNA Translation: CAA27827.1
U82664 Genomic DNA Translation: AAB40224.1
U00096 Genomic DNA Translation: AAC73572.1
U00096 Genomic DNA Translation: AYC08179.1
AP009048 Genomic DNA Translation: BAE76249.1
M38777 Genomic DNA Translation: AAA23457.1

Protein sequence database of the Protein Information Resource

More...PIRi		A25549 DJEC3G

NCBI Reference Sequences

More...RefSeqi		NP_415003.1, NC_000913.3
WP_000122013.1, NZ_SSUW01000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73572; AAC73572; b0470
BAE76249; BAE76249; BAE76249

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945105

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0459
eco:b0470

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1806

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04487 Genomic DNA Translation: CAA28174.1
X04487 Genomic DNA Translation: CAA28175.1 Different initiation.
X04275 Genomic DNA Translation: CAA27827.1
U82664 Genomic DNA Translation: AAB40224.1
U00096 Genomic DNA Translation: AAC73572.1
U00096 Genomic DNA Translation: AYC08179.1
AP009048 Genomic DNA Translation: BAE76249.1
M38777 Genomic DNA Translation: AAA23457.1
PIRiA25549 DJEC3G
RefSeqiNP_415003.1, NC_000913.3
WP_000122013.1, NZ_SSUW01000008.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JR3X-ray2.70A/B/C1-373[»]
1NJFX-ray2.30A/B/C/D1-243[»]
1NJGX-ray2.20A/B1-243[»]
1XXHX-ray3.45B/C/D/G/H/I1-373[»]
1XXIX-ray4.10B/C/D/G/H/I1-368[»]
2AYANMR-A499-625[»]
3GLFX-ray3.39B/C/D/G/H/I1-373[»]
3GLGX-ray3.25B/C/D/G/H/I1-373[»]
3GLHX-ray3.89B/C/D/G/H/I/L/M/N1-373[»]
3GLIX-ray3.50B/C/D/G/H/I1-373[»]
5FKUelectron microscopy8.34E500-643[»]
5FKVelectron microscopy8.00E500-643[»]
SMRiP06710
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4259846, 140 interactors
849494, 13 interactors
ComplexPortaliCPX-1926 DNA polymerase III clamp loader complex [P06710-2]
DIPiDIP-9464N
IntActiP06710, 33 interactors
STRINGi511145.b0470

Chemistry databases

BindingDBiP06710
DrugBankiDB02930 Adenosine 5'-[Gama-thio]triphosphate

Proteomic databases

EPDiP06710
jPOSTiP06710
PaxDbiP06710
PRIDEiP06710

Genome annotation databases

EnsemblBacteriaiAAC73572; AAC73572; b0470
BAE76249; BAE76249; BAE76249
GeneIDi945105
KEGGiecj:JW0459
eco:b0470
PATRICifig|1411691.4.peg.1806

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0241
EcoGeneiEG10245 dnaX

Phylogenomic databases

eggNOGiENOG4107QMP Bacteria
COG2812 LUCA
HOGENOMiHOG000083934
InParanoidiP06710
KOiK02343
PhylomeDBiP06710

Enzyme and pathway databases

BioCyciECOL316407:JW0459-MONOMER

Miscellaneous databases

EvolutionaryTraceiP06710

Protein Ontology

More...PROi		PR:P06710

Family and domain databases

Gene3Di3.30.300.150, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR001270 ClpA/B
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR022001 DNA_pol3_tau_IV
IPR022754 DNA_pol_III_gamma-3
IPR012763 DNA_pol_III_sug/sutau
IPR021029 DNA_pol_III_tau_dom-5
IPR027417 P-loop_NTPase
IPR038249 PolIII_tau_C_sf
PfamiView protein in Pfam
PF12169 DNA_pol3_gamma3, 1 hit
PF12168 DNA_pol3_tau_4, 1 hit
PF12170 DNA_pol3_tau_5, 1 hit
PRINTSiPR00300 CLPPROTEASEA
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF48019 SSF48019, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR02397 dnaX_nterm, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPO3X_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06710
Secondary accession number(s): A0A385XJC4, Q2MBV7, Q47721
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 16, 2019
This is version 189 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again