AC   MF_01152;
DC   Protein; auto
TR   HAMAP; MF_01152; -; 1; level=0
XX
Names: DnaJ
XX
ID   DNAJ
DE   RecName: Full=Chaperone protein DnaJ;
GN   Name=dnaJ;
XX
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC       heat shock by preventing the aggregation of stress-denatured proteins
CC       and by disaggregating proteins, also in an autonomous, DnaK-independent
CC       fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC       with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC       binding to DnaK triggers the release of the substrate protein, thus
CC       completing the reaction cycle. Several rounds of ATP-dependent
CC       interactions between DnaJ, DnaK and GrpE are required for fully
CC       efficient folding. Also involved, together with DnaK and GrpE, in the
CC       DNA replication of plasmids through activation of initiation proteins.
case <FTGroup:2> or <FTGroup:3>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per monomer.;
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC       ATPase activity. Zinc center 1 plays an important role in the
CC       autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC       is essential for interaction with DnaK and for DnaJ activity.
CC   -!- SIMILARITY: Belongs to the DnaJ family.
XX
DR   Pfam; PF00226; DnaJ; 1; trigger=no
DR   Pfam; PF01556; DnaJ_C; 1; trigger=no
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1; trigger=no
DR   PRINTS; PR00625; JDOMAIN; 1; trigger=no
DR   PROSITE; PS00636; DNAJ_1; 1; trigger=no
DR   PROSITE; PS50076; DNAJ_2; 1; trigger=yes
DR   PROSITE; PS51188; ZF_CR; 1; trigger=yes
DR   NCBIfam; TIGR02349; DnaJ_bact; 1; trigger=no
XX
KW   Cytoplasm
KW   Chaperone
KW   DNA replication
KW   Stress response
case <FTGroup:2> or <FTGroup:3>
KW   Metal-binding
end case
KW   Repeat
case <FTGroup:2> or <FTGroup:3>
KW   Zinc
end case
case <Feature:PS51188>
KW   Zinc-finger
end case
XX
GO   GO:0051082; F:unfolded protein binding
case <FTGroup:2> or <FTGroup:3>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: DNAJ_ECOLI (P08622)
FT   REPEAT          144..151
FT                   /note="CXXCXGXG motif"
FT   Group: 1; Condition: C-x(2)-C-x-G-x-G
FT   REPEAT          161..168
FT                   /note="CXXCXGXG motif"
FT   Group: 1; Condition: C-x(2)-C-x-G-x-G
FT   REPEAT          183..190
FT                   /note="CXXCXGXG motif"
FT   Group: 1; Condition: C-x(2)-C-x-G-x-G
FT   REPEAT          197..204
FT                   /note="CXXCXGXG motif"
FT   Group: 1; Condition: C-x(2)-C-x-G-x-G
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 2; Condition: C
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 2; Condition: C
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 2; Condition: C
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 2; Condition: C
XX
Size: 347-403;
Related: None;
Template: P08622;
Scope:
 Bacteria
 Archaea; Euryarchaeota
Fusion:
 Nter: None
 Cter: None
Duplicate: in AQUAE, AROAE, CORDI, COREF, CORGL, MYCBO, MYCLE, MYCPA, MYCTU,
 NOCFA, CUTAK, STRAL, STRAW, STRCO, SYNY3
Plasmid: None
Comments: None
XX
# Revision 1.25 2023/06/01
//