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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-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi144 – 1441Zinc 1
Metal bindingi147 – 1471Zinc 1
Metal bindingi161 – 1611Zinc 2
Metal bindingi164 – 1641Zinc 2
Metal bindingi183 – 1831Zinc 2
Metal bindingi186 – 1861Zinc 2
Metal bindingi197 – 1971Zinc 1
Metal bindingi200 – 2001Zinc 1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri131 – 20979CR-typeAdd
BLAST

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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 202RE → AA: No effect.
Mutagenesisi25 – 251Y → A: Loss of activity.
Mutagenesisi26 – 261K → A: Loss of activity.
Mutagenesisi27 – 271R → A: No effect.
Mutagenesisi28 – 281L → A: No effect.
Mutagenesisi29 – 291A → G: No effect.
Mutagenesisi30 – 312MK → AA: No effect.
Mutagenesisi32 – 321Y → A: No effect.
Mutagenesisi33 – 331H → Q: Loss of ability to stimulate DnaK ATPase activity. 1 Publication
Mutagenesisi34 – 341P → F: Loss of function.
Mutagenesisi35 – 351D → N: Loss of ability to bind DnaK. 1 Publication
Mutagenesisi36 – 361R → A: Decrease in chaperone function.
Mutagenesisi37 – 371N → A: Decrease in chaperone function.
Mutagenesisi38 – 381Q → A: No effect.
Mutagenesisi41 – 422KE → AA: No effect.
Mutagenesisi44 – 441E → A: No effect. 1 Publication
Mutagenesisi46 – 461K → A: No effect.
Mutagenesisi47 – 471F → A: Loss of function.
Mutagenesisi48 – 492KE → AA: No effect.
Mutagenesisi51 – 522KE → AA: No effect.
Mutagenesisi54 – 541Y → A: No effect. 1 Publication
Mutagenesisi55 – 551E → A: No effect. 1 Publication
Mutagenesisi58 – 592TD → AA: No effect.
Mutagenesisi60 – 612SQ → AA: No effect.
Mutagenesisi62 – 632KR → AA: No effect.
Mutagenesisi67 – 682DQ → AA: No effect.
Mutagenesisi144 – 1441C → S: Loss of DnaK-independent chaperone activity; when associated with S-147; S-197 and S-200. 1 Publication
Mutagenesisi147 – 1471C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-197 and S-200. 1 Publication
Mutagenesisi161 – 1611C → H: No effect on chaperone function; when associated with H-183. 2 Publications
Mutagenesisi161 – 1611C → S: Loss of function; when associated with S-164; S-183 and S-186. 2 Publications
Mutagenesisi164 – 1641C → H: No effect on chaperone function; when associated with H-183. 2 Publications
Mutagenesisi164 – 1641C → S: Loss of function; when associated with S-161; S-183 and S-186. 2 Publications
Mutagenesisi183 – 1831C → H: No effect on chaperone function. Same effect; when associated with H-161 or H-164. 2 Publications
Mutagenesisi183 – 1831C → S: Loss of function; when associated with S-161; S-164 and S-186. 2 Publications
Mutagenesisi186 – 1861C → H: No effect on chaperone function. 2 Publications
Mutagenesisi186 – 1861C → S: Loss of function; when associated with S-161; S-164 and S-184. 2 Publications
Mutagenesisi197 – 1971C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-200. 1 Publication
Mutagenesisi200 – 2001C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-197. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 376375Chaperone protein DnaJPRO_0000070777Add
BLAST

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 interactions.
849156. 1 interaction.
DIPiDIP-9460N.
IntActiP08622. 95 interactions.
MINTiMINT-1220303.
STRINGi511145.b0015.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 104Combined sources
Beta strandi13 – 153Combined sources
Helixi18 – 2912Combined sources
Turni30 – 323Combined sources
Turni34 – 363Combined sources
Turni38 – 403Combined sources
Helixi43 – 508Combined sources
Turni51 – 555Combined sources
Helixi61 – 655Combined sources
Turni66 – 683Combined sources
Turni70 – 723Combined sources
Turni132 – 1343Combined sources
Beta strandi141 – 1433Combined sources
Helixi145 – 1473Combined sources
Turni148 – 1503Combined sources
Beta strandi154 – 1563Combined sources
Turni162 – 1665Combined sources
Beta strandi167 – 1748Combined sources
Beta strandi177 – 1826Combined sources
Turni184 – 1885Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi194 – 1963Combined sources
Helixi198 – 2003Combined sources
Beta strandi203 – 2075Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQ0NMR-A2-104[»]
1BQZNMR-A2-78[»]
1EXKNMR-A131-209[»]
1XBLNMR-A2-108[»]
ProteinModelPortaliP08622.
SMRiP08622. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08622.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7270JAdd
BLAST
Repeati144 – 1518CXXCXGXG motif
Repeati161 – 1688CXXCXGXG motif
Repeati183 – 1908CXXCXGXG motif
Repeati197 – 2048CXXCXGXG motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 11438Gly-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri131 – 20979CR-typeAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQ0NMR-A2-104[»]
1BQZNMR-A2-78[»]
1EXKNMR-A131-209[»]
1XBLNMR-A2-108[»]
ProteinModelPortaliP08622.
SMRiP08622. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259725. 176 interactions.
849156. 1 interaction.
DIPiDIP-9460N.
IntActiP08622. 95 interactions.
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.

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: September 7, 2016
This is version 179 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.