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UniProtKB - P0A6Y8 (DNAK_ECOLI)

Entry version 143 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Chaperone protein DnaK

Gene

dnaK

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

Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

<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

  • ADP binding Source: EcoCyc
  • ATPase activity Source: CAFA
  • ATPase activity, coupled Source: GO_Central
  • ATP binding Source: CAFA
  • chaperone binding Source: CAFA
  • heat shock protein binding Source: GO_Central
  • misfolded protein binding Source: GO_Central
  • protein folding chaperone Source: EcoCyc
  • sigma factor antagonist activity Source: EcoCyc
  • unfolded protein binding Source: CAFA
  • zinc ion binding Source: EcoliWiki
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionChaperone
Biological processDNA replication, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10241-MONOMER
ECOL316407:JW0013-MONOMER
MetaCyc:EG10241-MONOMER

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.33.1.2 the cation channel-forming heat shock protein-70 (hsp70) family

<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:
Chaperone protein DnaK
Alternative name(s):
HSP70
Heat shock 70 kDa protein
Heat shock protein 70
<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:dnaK
Synonyms:groP, grpF, seg
Ordered Locus Names:b0014, JW0013
<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		EG10241 dnaK

<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

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at all at 43 degrees) and strain background.1 Publication

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>Mutagenesisi32G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. 2 Publications1
Mutagenesisi436V → I in SEG-2; confers temperature sensitivity. 1 Publication1
Mutagenesisi455G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication1
Mutagenesisi468G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication1

<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 methionineiRemoved3 Publications
<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_00000784582 – 638Chaperone protein DnaKAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei70N6-succinyllysine1 Publication1
Modified residuei109N6-acetyllysine1 Publication1
Modified residuei199Phosphothreonine; by autocatalysis2 Publications1
Modified residuei245N6-acetyllysine; alternate1 Publication1
Modified residuei245N6-succinyllysine; alternate1 Publication1
Modified residuei246N6-succinyllysine1 Publication1
Modified residuei304N6-acetyllysine; alternate1 Publication1
Modified residuei304N6-succinyllysine; alternate1 Publication1
Modified residuei359N6-succinyllysine1 Publication1
Modified residuei421N6-acetyllysine1 Publication1
Modified residuei502N6-succinyllysine1 Publication1
Modified residuei528N6-succinyllysine1 Publication1
Modified residuei556N6-acetyllysine1 Publication1
Modified residuei587N6-succinyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated; GrpE inhibits the autophosphorylation.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A6Y8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A6Y8

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

More...PaxDbi		P0A6Y8

PRoteomics IDEntifications database

More...PRIDEi		P0A6Y8

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0A6Y8

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P0A6Y8

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A6Y8

<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%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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259520, 182 interactors
849153, 10 interactors

Database of interacting proteins

More...DIPi		DIP-35751N

Protein interaction database and analysis system

More...IntActi		P0A6Y8, 379 interactors

Molecular INTeraction database

More...MINTi		P0A6Y8

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_0014

<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

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1BPRNMR-A384-561[»]
1DG4NMR-A393-507[»]
1DKGX-ray2.80D1-383[»]
1DKXX-ray2.00A389-607[»]
1DKYX-ray2.80A/B389-607[»]
1DKZX-ray2.00A389-607[»]
1Q5LNMR-A393-507[»]
2BPRNMR-A384-561[»]
2KHONMR-A1-605[»]
3DPOX-ray2.10A/B389-607[»]
3DPPX-ray2.50A/B389-607[»]
3DPQX-ray2.60A/B/E/F389-601[»]
3QNJX-ray2.28A/B389-607[»]
4B9QX-ray2.40A/B/C/D1-605[»]
4E81X-ray1.90A/B389-607[»]
4EZNX-ray1.80A/B389-607[»]
4EZOX-ray1.90A/B389-607[»]
4EZPX-ray1.65A/B389-607[»]
4EZQX-ray2.00A389-607[»]
4EZRX-ray1.90A389-607[»]
4EZSX-ray1.90A389-607[»]
4EZTX-ray2.00A389-607[»]
4EZUX-ray1.90A389-607[»]
4EZVX-ray2.10A/B389-607[»]
4EZWX-ray1.80A/B/C/D389-607[»]
4EZXX-ray1.70A/B389-607[»]
4EZYX-ray1.85A389-607[»]
4EZZX-ray2.05A389-607[»]
4F00X-ray1.95A389-607[»]
4F01X-ray1.40A/B389-607[»]
4HY9X-ray1.55A/B389-607[»]
4HYBX-ray1.70A/B389-607[»]
4JN4X-ray2.30A/B2-610[»]
4JNEX-ray1.96A/B2-610[»]
4JNFX-ray1.62A389-610[»]
4JWCX-ray1.80A/B389-607[»]
4JWDX-ray1.95A/B389-607[»]
4JWEX-ray1.95A/B389-607[»]
4JWIX-ray1.90A/B389-607[»]
4R5GX-ray3.45A/B389-607[»]
4R5IX-ray1.97A389-607[»]
4R5JX-ray2.36A/B/C/D389-607[»]
4R5KX-ray1.75A/B389-607[»]
4R5LX-ray2.97A/B/C/D389-607[»]
5NROX-ray3.25A1-605[»]
5OOWX-ray2.90A/B183-383[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0A6Y8

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

More...SMRi		P0A6Y8

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A6Y8

<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 heat shock protein 70 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CFG Bacteria
COG0443 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000228136

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A6Y8

KEGG Orthology (KO)

More...KOi		K04043

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A6Y8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.1270.10, 1 hit
2.60.34.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00332 DnaK, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012725 Chaperone_DnaK
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam

The PANTHER Classification System

More...PANTHERi		PTHR19375 PTHR19375, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00012 HSP70, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00301 HEATSHOCK70

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02350 prok_dnaK, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

P0A6Y8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV 
        60         70         80         90        100
GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD 
       110        120        130        140        150
AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ 
       160        170        180        190        200
RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF 
       210        220        230        240        250
DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI 
       260        270        280        290        300
DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 
       310        320        330        340        350
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ 
       360        370        380        390        400
KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG 
       410        420        430        440        450
IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD 
       460        470        480        490        500
NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT 
       510        520        530        540        550
IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV 
       560        570        580        590        600
EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 
       610        620        630 
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
Length:638
Mass (Da):69,115
Last modified:January 23, 2007 - v2
<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:i5A8589B21D7CD9C1
GO

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
K01298 Genomic DNA Translation: AAA23694.1
U00096 Genomic DNA Translation: AAC73125.1
AP009048 Genomic DNA Translation: BAB96589.1
D10765 Genomic DNA Translation: BAA01595.1
M12565 Genomic DNA Translation: AAA23692.1

Protein sequence database of the Protein Information Resource

More...PIRi		A03311 IQECDK

NCBI Reference Sequences

More...RefSeqi		NP_414555.1, NC_000913.3
WP_000516135.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73125; AAC73125; b0014
BAB96589; BAB96589; BAB96589

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944750

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0013
eco:b0014

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2270

<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
K01298 Genomic DNA Translation: AAA23694.1
U00096 Genomic DNA Translation: AAC73125.1
AP009048 Genomic DNA Translation: BAB96589.1
D10765 Genomic DNA Translation: BAA01595.1
M12565 Genomic DNA Translation: AAA23692.1
PIRiA03311 IQECDK
RefSeqiNP_414555.1, NC_000913.3
WP_000516135.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BPRNMR-A384-561[»]
1DG4NMR-A393-507[»]
1DKGX-ray2.80D1-383[»]
1DKXX-ray2.00A389-607[»]
1DKYX-ray2.80A/B389-607[»]
1DKZX-ray2.00A389-607[»]
1Q5LNMR-A393-507[»]
2BPRNMR-A384-561[»]
2KHONMR-A1-605[»]
3DPOX-ray2.10A/B389-607[»]
3DPPX-ray2.50A/B389-607[»]
3DPQX-ray2.60A/B/E/F389-601[»]
3QNJX-ray2.28A/B389-607[»]
4B9QX-ray2.40A/B/C/D1-605[»]
4E81X-ray1.90A/B389-607[»]
4EZNX-ray1.80A/B389-607[»]
4EZOX-ray1.90A/B389-607[»]
4EZPX-ray1.65A/B389-607[»]
4EZQX-ray2.00A389-607[»]
4EZRX-ray1.90A389-607[»]
4EZSX-ray1.90A389-607[»]
4EZTX-ray2.00A389-607[»]
4EZUX-ray1.90A389-607[»]
4EZVX-ray2.10A/B389-607[»]
4EZWX-ray1.80A/B/C/D389-607[»]
4EZXX-ray1.70A/B389-607[»]
4EZYX-ray1.85A389-607[»]
4EZZX-ray2.05A389-607[»]
4F00X-ray1.95A389-607[»]
4F01X-ray1.40A/B389-607[»]
4HY9X-ray1.55A/B389-607[»]
4HYBX-ray1.70A/B389-607[»]
4JN4X-ray2.30A/B2-610[»]
4JNEX-ray1.96A/B2-610[»]
4JNFX-ray1.62A389-610[»]
4JWCX-ray1.80A/B389-607[»]
4JWDX-ray1.95A/B389-607[»]
4JWEX-ray1.95A/B389-607[»]
4JWIX-ray1.90A/B389-607[»]
4R5GX-ray3.45A/B389-607[»]
4R5IX-ray1.97A389-607[»]
4R5JX-ray2.36A/B/C/D389-607[»]
4R5KX-ray1.75A/B389-607[»]
4R5LX-ray2.97A/B/C/D389-607[»]
5NROX-ray3.25A1-605[»]
5OOWX-ray2.90A/B183-383[»]
ProteinModelPortaliP0A6Y8
SMRiP0A6Y8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259520, 182 interactors
849153, 10 interactors
DIPiDIP-35751N
IntActiP0A6Y8, 379 interactors
MINTiP0A6Y8
STRINGi316385.ECDH10B_0014

Protein family/group databases

TCDBi1.A.33.1.2 the cation channel-forming heat shock protein-70 (hsp70) family

PTM databases

CarbonylDBiP0A6Y8
iPTMnetiP0A6Y8

2D gel databases

SWISS-2DPAGEiP0A6Y8

Proteomic databases

EPDiP0A6Y8
jPOSTiP0A6Y8
PaxDbiP0A6Y8
PRIDEiP0A6Y8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73125; AAC73125; b0014
BAB96589; BAB96589; BAB96589
GeneIDi944750
KEGGiecj:JW0013
eco:b0014
PATRICifig|1411691.4.peg.2270

Organism-specific databases

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

More...EchoBASEi		EB0237
EcoGeneiEG10241 dnaK

Phylogenomic databases

eggNOGiENOG4105CFG Bacteria
COG0443 LUCA
HOGENOMiHOG000228136
InParanoidiP0A6Y8
KOiK04043
PhylomeDBiP0A6Y8

Enzyme and pathway databases

BioCyciEcoCyc:EG10241-MONOMER
ECOL316407:JW0013-MONOMER
MetaCyc:EG10241-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A6Y8

Protein Ontology

More...PROi		PR:P0A6Y8

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
HAMAPiMF_00332 DnaK, 1 hit
InterProiView protein in InterPro
IPR012725 Chaperone_DnaK
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
TIGRFAMsiTIGR02350 prok_dnaK, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiDNAK_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: P0A6Y8
Secondary accession number(s): P04475
<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: August 13, 1987
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 143 of the entry and version 2 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
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