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Protein

Chaperone protein DnaJ

Gene

dnaJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Cofactori

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

Sites

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processDNA replication, Stress response
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10240-MONOMER
MetaCyc:EG10240-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein DnaJ
Alternative name(s):
HSP40
Heat shock protein J
Gene namesi
Name:dnaJ
Synonyms:groP
Ordered Locus Names:b0015, JW0014
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10240 dnaJ

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

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
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000707772 – 376Chaperone protein DnaJAdd BLAST375

Proteomic databases

EPDiP08622
PaxDbiP08622
PRIDEiP08622

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4259725, 278 interactors
849156, 2 interactors
DIPiDIP-9460N
IntActiP08622, 101 interactors
MINTiP08622
STRINGi316385.ECDH10B_0015

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP08622
SMRiP08622
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08622

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 72JAdd BLAST70
Repeati144 – 151CXXCXGXG motif8
Repeati161 – 168CXXCXGXG motif8
Repeati183 – 190CXXCXGXG motif8
Repeati197 – 204CXXCXGXG motif8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi77 – 114Gly-richAdd BLAST38

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.

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

eggNOGiENOG4105BZ5 Bacteria
COG0484 LUCA
HOGENOMiHOG000226717
InParanoidiP08622
KOiK03686
PhylomeDBiP08622

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

Sequencei

Sequence statusi: Complete.

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
Checksum:i05FA762EF9844532
GO

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

Genome annotation databases

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

Similar proteinsi

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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQ0NMR-A2-104[»]
1BQZNMR-A2-78[»]
1EXKNMR-A131-209[»]
1XBLNMR-A2-108[»]
5NROX-ray3.25B1-105[»]
ProteinModelPortaliP08622
SMRiP08622
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259725, 278 interactors
849156, 2 interactors
DIPiDIP-9460N
IntActiP08622, 101 interactors
MINTiP08622
STRINGi316385.ECDH10B_0015

Proteomic databases

EPDiP08622
PaxDbiP08622
PRIDEiP08622

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0236
EcoGeneiEG10240 dnaJ

Phylogenomic databases

eggNOGiENOG4105BZ5 Bacteria
COG0484 LUCA
HOGENOMiHOG000226717
InParanoidiP08622
KOiK03686
PhylomeDBiP08622

Enzyme and pathway databases

BioCyciEcoCyc:EG10240-MONOMER
MetaCyc:EG10240-MONOMER

Miscellaneous databases

EvolutionaryTraceiP08622
PROiPR: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
ProtoNetiSearch...

Entry informationi

Entry nameiDNAJ_ECOLI
AccessioniPrimary (citable) accession number: P08622
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 194 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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

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