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HAMAP rule MF_01152

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01152
Accession MF_01152
Dates 12-APR-2005 (Created)
8-OCT-2024 (Last updated, Version 26)
Name DnaJ
Scope(s) Bacteria
Archaea
Methanobacteriati
Template(s) P08622 (DNAJ_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_01152 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier DNAJ
Protein name RecName: Full=Chaperone protein DnaJ;
Gene name Name=dnaJ;

Comments [?]

FUNCTIONParticipates 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
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
DOMAINThe 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.
SIMILARITYBelongs to the DnaJ family.

Keywords [?]

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 [?]

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 [?]

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 [?]

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 [?]

Size range 347-403 amino acids
Related rules None
Fusion Nter: None Cter: None



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