Skip Header

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

Chaperone protein DnaJ

Gene

dnaJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • ATP binding Source: InterPro
  • protein disulfide isomerase activity Source: EcoliWiki
  • protein disulfide oxidoreductase activity Source: EcoCyc
  • sigma factor antagonist activity Source: EcoCyc
  • unfolded protein binding Source: EcoliWiki
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • chaperone cofactor-dependent protein refolding Source: EcoCyc
  • DNA replication Source: EcoliWiki
  • protein folding Source: EcoliWiki
  • protein refolding Source: EcoliWiki
  • response to heat Source: EcoCyc
  • viral process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

DNA replication, Stress response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10240-MONOMER.
ECOL316407:JW0014-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

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
  • membrane Source: EcoliWiki
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
dnaKP0A6Y85EBI-545285,EBI-542092
malTP069933EBI-545285,EBI-542934

GO - Molecular functioni

  • unfolded protein binding Source: EcoliWiki

Protein-protein interaction databases

BioGridi4259725. 176 interactors.
849156. 1 interactor.
DIPiDIP-9460N.
IntActiP08622. 95 interactors.
MINTiMINT-1220303.
STRINGi511145.b0015.

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 10Combined sources4
Beta strandi13 – 15Combined sources3
Helixi18 – 29Combined sources12
Turni30 – 32Combined sources3
Turni34 – 36Combined sources3
Turni38 – 40Combined sources3
Helixi43 – 50Combined sources8
Turni51 – 55Combined sources5
Helixi61 – 65Combined sources5
Turni66 – 68Combined sources3
Turni70 – 72Combined sources3
Turni132 – 134Combined sources3
Beta strandi141 – 143Combined sources3
Helixi145 – 147Combined sources3
Turni148 – 150Combined sources3
Beta strandi154 – 156Combined sources3
Turni162 – 166Combined sources5
Beta strandi167 – 174Combined sources8
Beta strandi177 – 182Combined sources6
Turni184 – 188Combined sources5
Beta strandi189 – 192Combined sources4
Beta strandi194 – 196Combined sources3
Helixi198 – 200Combined sources3
Beta strandi203 – 207Combined sources5

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[»]
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
Contains 1 CR-type zinc finger.Curated
Contains 1 J domain.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.
OMAiIKDPCNS.
PhylomeDBiP08622.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
TIGRFAMsiTIGR02349. DnaJ_bact. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

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.
PATRICi32115123. VBIEscCol129921_0013.

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[»]
ProteinModelPortaliP08622.
SMRiP08622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259725. 176 interactors.
849156. 1 interactor.
DIPiDIP-9460N.
IntActiP08622. 95 interactors.
MINTiMINT-1220303.
STRINGi511145.b0015.

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.
PATRICi32115123. VBIEscCol129921_0013.

Organism-specific databases

EchoBASEiEB0236.
EcoGeneiEG10240. dnaJ.

Phylogenomic databases

eggNOGiENOG4105BZ5. Bacteria.
COG0484. LUCA.
HOGENOMiHOG000226717.
InParanoidiP08622.
KOiK03686.
OMAiIKDPCNS.
PhylomeDBiP08622.

Enzyme and pathway databases

BioCyciEcoCyc:EG10240-MONOMER.
ECOL316407:JW0014-MONOMER.
MetaCyc:EG10240-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP08622.
PROiP08622.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
TIGRFAMsiTIGR02349. DnaJ_bact. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNAJ_ECOLI
AccessioniPrimary (citable) accession number: P08622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 181 of the entry and version 3 of the sequence. [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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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