HAMAP rule MF_01152
General rule information
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Accession | MF_01152 |
Dates | 12-APR-2005 (Created)
1-JUN-2023 (Last updated, Version 25) |
Name | DnaJ |
Scope(s) |
Bacteria Archaea Euryarchaeota |
Template(s) | P08622 (DNAJ_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01152 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | DNAJ |
Protein name | RecName: Full=Chaperone protein DnaJ; |
Gene name | Name=dnaJ; |
Comments
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FUNCTION | 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. |
case <FTGroup:2> or <FTGroup:3> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per monomer.; |
end case | |
SUBUNIT | Homodimer. |
SUBCELLULAR LOCATION | Cytoplasm. |
DOMAIN | 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. |
SIMILARITY | Belongs to the DnaJ family. |
Keywords
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Cytoplasm | |
Chaperone | |
DNA replication | |
Stress response | |
case <FTGroup:2> or <FTGroup:3> | |
Metal-binding | |
end case | |
Repeat | |
case <FTGroup:2> or <FTGroup:3> | |
Zinc | |
end case | |
case <Feature:PS51188> | |
Zinc-finger | |
end case |
Gene Ontology
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GO:0051082; Molecular function:unfolded protein binding | |
case <FTGroup:2> or <FTGroup:3> | |
GO:0008270; Molecular function:zinc ion binding | |
end case | |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Pfam | PF00226; DnaJ; 1; |
Pfam | PF01556; DnaJ_C; 1; |
Pfam | PF00684; DnaJ_CXXCXGXG; 1; |
PRINTS | PR00625; JDOMAIN; 1; |
PROSITE | PS00636; DNAJ_1; 1; |
PROSITE | PS50076; DNAJ_2; 1; |
PROSITE | PS51188; ZF_CR; 1; |
NCBIfam | TIGR02349; DnaJ_bact; 1; |
Features
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From: DNAJ_ECOLI (P08622) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REPEAT | 144 | 151 | /note="CXXCXGXG motif" | C-x(2)-C-x-G-x-G | 1 | |||||||
REPEAT | 161 | 168 | /note="CXXCXGXG motif" | C-x(2)-C-x-G-x-G | 1 | |||||||
REPEAT | 183 | 190 | /note="CXXCXGXG motif" | C-x(2)-C-x-G-x-G | 1 | |||||||
REPEAT | 197 | 204 | /note="CXXCXGXG motif" | C-x(2)-C-x-G-x-G | 1 | |||||||
BINDING | 144 | 144 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | 2 | |||||||
BINDING | 147 | 147 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | 2 | |||||||
BINDING | 161 | 161 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | 3 | |||||||
BINDING | 164 | 164 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | 3 | |||||||
BINDING | 183 | 183 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | 3 | |||||||
BINDING | 186 | 186 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | 3 | |||||||
BINDING | 197 | 197 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | 2 | |||||||
BINDING | 200 | 200 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | 2 |
Additional information
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Size range | 347-403 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |