UniProtKB - P08622 (DNAJ_ECOLI)
Chaperone protein DnaJ
dnaJ
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 PublicationsCofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 144 | Zinc 1 | 1 | |
Metal bindingi | 147 | Zinc 1 | 1 | |
Metal bindingi | 161 | Zinc 2 | 1 | |
Metal bindingi | 164 | Zinc 2 | 1 | |
Metal bindingi | 183 | Zinc 2 | 1 | |
Metal bindingi | 186 | Zinc 2 | 1 | |
Metal bindingi | 197 | Zinc 1 | 1 | |
Metal bindingi | 200 | Zinc 1 | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 131 – 209 | CR-typeAdd BLAST | 79 |
GO - Molecular functioni
- ATP binding Source: InterPro
- chaperone binding Source: CAFA
- heat shock protein binding Source: InterPro
- protein disulfide isomerase activity Source: EcoliWiki
- protein-disulfide reductase activity Source: EcoCyc
- sigma factor antagonist activity Source: EcoCyc
- unfolded protein binding Source: CAFA
- zinc ion binding Source: EcoliWiki
GO - Biological processi
- chaperone cofactor-dependent protein refolding Source: CAFA
- DNA replication Source: EcoliWiki
- protein-containing complex assembly Source: CAFA
- protein folding Source: EcoliWiki
- protein refolding Source: EcoliWiki
- response to heat Source: EcoCyc
- viral process Source: EcoCyc
Keywordsi
Molecular function | Chaperone |
Biological process | DNA replication, Stress response |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10240-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Chaperone protein DnaJAlternative name(s): HSP40 Heat shock protein J |
Gene namesi | Name:dnaJ Synonyms:groP Ordered Locus Names:b0015, JW0014 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
Cytosol
- cytosol Source: EcoCyc
Other locations
- cytoplasm Source: EcoliWiki
- membrane Source: EcoliWiki
- protein-containing complex Source: CAFA
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 19 – 20 | RE → AA: No effect. | 2 | |
Mutagenesisi | 25 | Y → A: Loss of activity. | 1 | |
Mutagenesisi | 26 | K → A: Loss of activity. | 1 | |
Mutagenesisi | 27 | R → A: No effect. | 1 | |
Mutagenesisi | 28 | L → A: No effect. | 1 | |
Mutagenesisi | 29 | A → G: No effect. | 1 | |
Mutagenesisi | 30 – 31 | MK → AA: No effect. | 2 | |
Mutagenesisi | 32 | Y → A: No effect. | 1 | |
Mutagenesisi | 33 | H → Q: Loss of ability to stimulate DnaK ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 34 | P → F: Loss of function. | 1 | |
Mutagenesisi | 35 | D → N: Loss of ability to bind DnaK. 1 Publication | 1 | |
Mutagenesisi | 36 | R → A: Decrease in chaperone function. | 1 | |
Mutagenesisi | 37 | N → A: Decrease in chaperone function. | 1 | |
Mutagenesisi | 38 | Q → A: No effect. | 1 | |
Mutagenesisi | 41 – 42 | KE → AA: No effect. | 2 | |
Mutagenesisi | 44 | E → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 46 | K → A: No effect. | 1 | |
Mutagenesisi | 47 | F → A: Loss of function. | 1 | |
Mutagenesisi | 48 – 49 | KE → AA: No effect. | 2 | |
Mutagenesisi | 51 – 52 | KE → AA: No effect. | 2 | |
Mutagenesisi | 54 | Y → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 55 | E → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 58 – 59 | TD → AA: No effect. | 2 | |
Mutagenesisi | 60 – 61 | SQ → AA: No effect. | 2 | |
Mutagenesisi | 62 – 63 | KR → AA: No effect. | 2 | |
Mutagenesisi | 67 – 68 | DQ → AA: No effect. | 2 | |
Mutagenesisi | 144 | C → S: Loss of DnaK-independent chaperone activity; when associated with S-147; S-197 and S-200. 1 Publication | 1 | |
Mutagenesisi | 147 | C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-197 and S-200. 1 Publication | 1 | |
Mutagenesisi | 161 | C → H: No effect on chaperone function; when associated with H-183. 2 Publications | 1 | |
Mutagenesisi | 161 | C → S: Loss of function; when associated with S-164; S-183 and S-186. 2 Publications | 1 | |
Mutagenesisi | 164 | C → H: No effect on chaperone function; when associated with H-183. 2 Publications | 1 | |
Mutagenesisi | 164 | C → S: Loss of function; when associated with S-161; S-183 and S-186. 2 Publications | 1 | |
Mutagenesisi | 183 | C → H: No effect on chaperone function. Same effect; when associated with H-161 or H-164. 2 Publications | 1 | |
Mutagenesisi | 183 | C → S: Loss of function; when associated with S-161; S-164 and S-186. 2 Publications | 1 | |
Mutagenesisi | 186 | C → H: No effect on chaperone function. 2 Publications | 1 | |
Mutagenesisi | 186 | C → S: Loss of function; when associated with S-161; S-164 and S-184. 2 Publications | 1 | |
Mutagenesisi | 197 | C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-200. 1 Publication | 1 | |
Mutagenesisi | 200 | C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-197. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000070777 | 2 – 376 | Chaperone protein DnaJAdd BLAST | 375 |
Proteomic databases
jPOSTi | P08622 |
PaxDbi | P08622 |
PRIDEi | P08622 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Homodimer.
Binary interactionsi
GO - Molecular functioni
- chaperone binding Source: CAFA
- heat shock protein binding Source: InterPro
- unfolded protein binding Source: CAFA
Protein-protein interaction databases
BioGRIDi | 4259725, 278 interactors 849156, 3 interactors |
DIPi | DIP-9460N |
IntActi | P08622, 101 interactors |
MINTi | P08622 |
STRINGi | 511145.b0015 |
Structurei
Secondary structure
3D structure databases
SMRi | P08622 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08622 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 3 – 72 | JAdd BLAST | 70 | |
Repeati | 144 – 151 | CXXCXGXG motif | 8 | |
Repeati | 161 – 168 | CXXCXGXG motif | 8 | |
Repeati | 183 – 190 | CXXCXGXG motif | 8 | |
Repeati | 197 – 204 | CXXCXGXG motif | 8 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 131 – 209 | CR-typeAdd BLAST | 79 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | COG0484, Bacteria |
HOGENOMi | CLU_017633_0_7_6 |
InParanoidi | P08622 |
PhylomeDBi | P08622 |
Family and domain databases
CDDi | cd06257, DnaJ, 1 hit cd10719, DnaJ_zf, 1 hit |
Gene3Di | 1.10.287.110, 1 hit |
HAMAPi | MF_01152, DnaJ, 1 hit |
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 |
Pfami | View protein in Pfam PF00226, DnaJ, 1 hit PF01556, DnaJ_C, 1 hit PF00684, DnaJ_CXXCXGXG, 1 hit |
PRINTSi | PR00625, JDOMAIN |
SMARTi | View protein in SMART SM00271, DnaJ, 1 hit |
SUPFAMi | SSF46565, SSF46565, 1 hit SSF49493, SSF49493, 2 hits SSF57938, SSF57938, 1 hit |
TIGRFAMsi | TIGR02349, DnaJ_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00636, DNAJ_1, 1 hit PS50076, DNAJ_2, 1 hit PS51188, ZF_CR, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
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 |
PIRi | A92572, HHECDJ |
RefSeqi | NP_414556.1, NC_000913.3 WP_001118476.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC73126; AAC73126; b0015 BAB96590; BAB96590; BAB96590 |
GeneIDi | 944753 |
KEGGi | ecj:JW0014 eco:b0015 |
PATRICi | fig|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 |
PIRi | A92572, HHECDJ |
RefSeqi | NP_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 entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BQ0 | NMR | - | A | 2-104 | [»] | |
1BQZ | NMR | - | A | 2-78 | [»] | |
1EXK | NMR | - | A | 131-209 | [»] | |
1XBL | NMR | - | A | 2-108 | [»] | |
5NRO | X-ray | 3.25 | B | 1-105 | [»] | |
SMRi | P08622 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259725, 278 interactors 849156, 3 interactors |
DIPi | DIP-9460N |
IntActi | P08622, 101 interactors |
MINTi | P08622 |
STRINGi | 511145.b0015 |
Proteomic databases
jPOSTi | P08622 |
PaxDbi | P08622 |
PRIDEi | P08622 |
Genome annotation databases
EnsemblBacteriai | AAC73126; AAC73126; b0015 BAB96590; BAB96590; BAB96590 |
GeneIDi | 944753 |
KEGGi | ecj:JW0014 eco:b0015 |
PATRICi | fig|1411691.4.peg.2269 |
Organism-specific databases
EchoBASEi | EB0236 |
Phylogenomic databases
eggNOGi | COG0484, Bacteria |
HOGENOMi | CLU_017633_0_7_6 |
InParanoidi | P08622 |
PhylomeDBi | P08622 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10240-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P08622 |
PROi | PR:P08622 |
Family and domain databases
CDDi | cd06257, DnaJ, 1 hit cd10719, DnaJ_zf, 1 hit |
Gene3Di | 1.10.287.110, 1 hit |
HAMAPi | MF_01152, DnaJ, 1 hit |
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 |
Pfami | View protein in Pfam PF00226, DnaJ, 1 hit PF01556, DnaJ_C, 1 hit PF00684, DnaJ_CXXCXGXG, 1 hit |
PRINTSi | PR00625, JDOMAIN |
SMARTi | View protein in SMART SM00271, DnaJ, 1 hit |
SUPFAMi | SSF46565, SSF46565, 1 hit SSF49493, SSF49493, 2 hits SSF57938, SSF57938, 1 hit |
TIGRFAMsi | TIGR02349, DnaJ_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00636, DNAJ_1, 1 hit PS50076, DNAJ_2, 1 hit PS51188, ZF_CR, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DNAJ_ECOLI | |
Accessioni | P08622Primary (citable) accession number: P08622 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families