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UniProtKB - P08622 (DNAJ_ECOLI)

Entry version 211 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Chaperone protein DnaJ

Gene

dnaJ

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

Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

4 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 2 Zn2+ ions per monomer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi144Zinc 11
Metal bindingi147Zinc 11
Metal bindingi161Zinc 21
Metal bindingi164Zinc 21
Metal bindingi183Zinc 21
Metal bindingi186Zinc 21
Metal bindingi197Zinc 11
Metal bindingi200Zinc 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri131 – 209CR-typeAdd BLAST79

<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

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
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10240-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%5Fand%5Ftaxonomy%5Fsection">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 DnaJ
Alternative name(s):
HSP40
Heat shock protein J
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:dnaJ
Synonyms:groP
Ordered Locus Names:b0015, JW0014
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

Keywords - Cellular componenti

Cytoplasm

<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

Single dnaJ and double dnaK-dnaJ disruption are 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 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi19 – 20RE → AA: No effect. 2
Mutagenesisi25Y → A: Loss of activity. 1
Mutagenesisi26K → A: Loss of activity. 1
Mutagenesisi27R → A: No effect. 1
Mutagenesisi28L → A: No effect. 1
Mutagenesisi29A → G: No effect. 1
Mutagenesisi30 – 31MK → AA: No effect. 2
Mutagenesisi32Y → A: No effect. 1
Mutagenesisi33H → Q: Loss of ability to stimulate DnaK ATPase activity. 1 Publication1
Mutagenesisi34P → F: Loss of function. 1
Mutagenesisi35D → N: Loss of ability to bind DnaK. 1 Publication1
Mutagenesisi36R → A: Decrease in chaperone function. 1
Mutagenesisi37N → A: Decrease in chaperone function. 1
Mutagenesisi38Q → A: No effect. 1
Mutagenesisi41 – 42KE → AA: No effect. 2
Mutagenesisi44E → A: No effect. 1 Publication1
Mutagenesisi46K → A: No effect. 1
Mutagenesisi47F → A: Loss of function. 1
Mutagenesisi48 – 49KE → AA: No effect. 2
Mutagenesisi51 – 52KE → AA: No effect. 2
Mutagenesisi54Y → A: No effect. 1 Publication1
Mutagenesisi55E → A: No effect. 1 Publication1
Mutagenesisi58 – 59TD → AA: No effect. 2
Mutagenesisi60 – 61SQ → AA: No effect. 2
Mutagenesisi62 – 63KR → AA: No effect. 2
Mutagenesisi67 – 68DQ → AA: No effect. 2
Mutagenesisi144C → S: Loss of DnaK-independent chaperone activity; when associated with S-147; S-197 and S-200. 1 Publication1
Mutagenesisi147C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-197 and S-200. 1 Publication1
Mutagenesisi161C → H: No effect on chaperone function; when associated with H-183. 2 Publications1
Mutagenesisi161C → S: Loss of function; when associated with S-164; S-183 and S-186. 2 Publications1
Mutagenesisi164C → H: No effect on chaperone function; when associated with H-183. 2 Publications1
Mutagenesisi164C → S: Loss of function; when associated with S-161; S-183 and S-186. 2 Publications1
Mutagenesisi183C → H: No effect on chaperone function. Same effect; when associated with H-161 or H-164. 2 Publications1
Mutagenesisi183C → S: Loss of function; when associated with S-161; S-164 and S-186. 2 Publications1
Mutagenesisi186C → H: No effect on chaperone function. 2 Publications1
Mutagenesisi186C → S: Loss of function; when associated with S-161; S-164 and S-184. 2 Publications1
Mutagenesisi197C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-200. 1 Publication1
Mutagenesisi200C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-197. 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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000707772 – 376Chaperone protein DnaJAdd BLAST375

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08622

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

More...PaxDbi		P08622

PRoteomics IDEntifications database

More...PRIDEi		P08622

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock under the control of the HtpR regulatory protein.

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259725, 278 interactors
849156, 3 interactors

Database of interacting proteins

More...DIPi		DIP-9460N

Protein interaction database and analysis system

More...IntActi		P08622, 101 interactors

Molecular INTeraction database

More...MINTi		P08622

STRING: functional protein association networks

More...STRINGi		511145.b0015

<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

1376
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		P08622

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		P08622

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 72JAdd BLAST70
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati144 – 151CXXCXGXG motif8
Repeati161 – 168CXXCXGXG motif8
Repeati183 – 190CXXCXGXG motif8
Repeati197 – 204CXXCXGXG motif8

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.

<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 DnaJ family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri131 – 209CR-typeAdd BLAST79

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0484, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_017633_0_7_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08622

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08622

Family and domain databases

Conserved Domains Database

More...CDDi		cd06257, DnaJ, 1 hit
cd10719, DnaJ_zf, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.287.110, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01152, DnaJ, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012724, DnaJ
IPR002939, DnaJ_C
IPR001623, DnaJ_domain
IPR018253, DnaJ_domain_CS
IPR008971, HSP40/DnaJ_pept-bd
IPR001305, HSP_DnaJ_Cys-rich_dom
IPR036410, HSP_DnaJ_Cys-rich_dom_sf
IPR036869, J_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00226, DnaJ, 1 hit
PF01556, DnaJ_C, 1 hit
PF00684, DnaJ_CXXCXGXG, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00625, JDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00271, DnaJ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46565, SSF46565, 1 hit
SSF49493, SSF49493, 2 hits
SSF57938, SSF57938, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02349, DnaJ_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00636, DNAJ_1, 1 hit
PS50076, DNAJ_2, 1 hit
PS51188, ZF_CR, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P08622-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI 
        60         70         80         90        100
KEAYEVLTDS QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD 
       110        120        130        140        150
IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT LEECDVCHGS 
       160        170        180        190        200
GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC 
       210        220        230        240        250
HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP AGDLYVQVQV 
       260        270        280        290        300
KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG 
       310        320        330        340        350
KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG 
       360        370 
PTGEHNSPRS KSFFDGVKKF FDDLTR
Length:376
Mass (Da):41,100
Last modified:January 23, 2007 - v3
<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:i05FA762EF9844532
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
M12544 Genomic DNA Translation: AAA00009.1
M12565 Genomic DNA Translation: AAA23693.1
U00096 Genomic DNA Translation: AAC73126.1
AP009048 Genomic DNA Translation: BAB96590.1

Protein sequence database of the Protein Information Resource

More...PIRi		A92572, HHECDJ

NCBI Reference Sequences

More...RefSeqi		NP_414556.1, NC_000913.3
WP_001118476.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73126; AAC73126; b0015
BAB96590; BAB96590; BAB96590

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944753

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0014
eco:b0015

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2269

<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
M12544 Genomic DNA Translation: AAA00009.1
M12565 Genomic DNA Translation: AAA23693.1
U00096 Genomic DNA Translation: AAC73126.1
AP009048 Genomic DNA Translation: BAB96590.1
PIRiA92572, HHECDJ
RefSeqiNP_414556.1, NC_000913.3
WP_001118476.1, NZ_LN832404.1

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
1BQ0NMR-A2-104[»]
1BQZNMR-A2-78[»]
1EXKNMR-A131-209[»]
1XBLNMR-A2-108[»]
5NROX-ray3.25B1-105[»]
SMRiP08622
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259725, 278 interactors
849156, 3 interactors
DIPiDIP-9460N
IntActiP08622, 101 interactors
MINTiP08622
STRINGi511145.b0015

Proteomic databases

jPOSTiP08622
PaxDbiP08622
PRIDEiP08622

Genome annotation databases

EnsemblBacteriaiAAC73126; AAC73126; b0015
BAB96590; BAB96590; BAB96590
GeneIDi944753
KEGGiecj:JW0014
eco:b0015
PATRICifig|1411691.4.peg.2269

Organism-specific databases

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

More...EchoBASEi		EB0236

Phylogenomic databases

eggNOGiCOG0484, Bacteria
HOGENOMiCLU_017633_0_7_6
InParanoidiP08622
PhylomeDBiP08622

Enzyme and pathway databases

BioCyciEcoCyc:EG10240-MONOMER

Miscellaneous databases

EvolutionaryTraceiP08622

Protein Ontology

More...PROi		PR:P08622

Family and domain databases

CDDicd06257, DnaJ, 1 hit
cd10719, DnaJ_zf, 1 hit
Gene3Di1.10.287.110, 1 hit
HAMAPiMF_01152, DnaJ, 1 hit
InterProiView protein in InterPro
IPR012724, DnaJ
IPR002939, DnaJ_C
IPR001623, DnaJ_domain
IPR018253, DnaJ_domain_CS
IPR008971, HSP40/DnaJ_pept-bd
IPR001305, HSP_DnaJ_Cys-rich_dom
IPR036410, HSP_DnaJ_Cys-rich_dom_sf
IPR036869, J_dom_sf
PfamiView protein in Pfam
PF00226, DnaJ, 1 hit
PF01556, DnaJ_C, 1 hit
PF00684, DnaJ_CXXCXGXG, 1 hit
PRINTSiPR00625, JDOMAIN
SMARTiView protein in SMART
SM00271, DnaJ, 1 hit
SUPFAMiSSF46565, SSF46565, 1 hit
SSF49493, SSF49493, 2 hits
SSF57938, SSF57938, 1 hit
TIGRFAMsiTIGR02349, DnaJ_bact, 1 hit
PROSITEiView protein in PROSITE
PS00636, DNAJ_1, 1 hit
PS50076, DNAJ_2, 1 hit
PS51188, ZF_CR, 1 hit

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 nameiDNAJ_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: P08622
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 211 of the entry and version 3 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, 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
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