STRINGSTRING
dnaJ dnaJ AFY79528.1 AFY79528.1 AFY79411.1 AFY79411.1 AFY79372.1 AFY79372.1 AFY79201.1 AFY79201.1 AFY79089.1 AFY79089.1 AFY78903.1 AFY78903.1 AFY78654.1 AFY78654.1 AFY78412.1 AFY78412.1 AFY77924.1 AFY77924.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
dnaJChaperone protein DnaJ; 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, D [...] (375 aa)
AFY79528.1Putative low-complexity protein; PFAM: Pentapeptide repeats (8 copies); DnaJ domain. (225 aa)
AFY79411.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. (303 aa)
AFY79372.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. (233 aa)
AFY79201.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. (164 aa)
AFY79089.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. (357 aa)
AFY78903.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. (331 aa)
AFY78654.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain. (335 aa)
AFY78412.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. (770 aa)
AFY77924.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. (295 aa)
Your Current Organism:
Pleurocapsa sp. PCC7327
NCBI taxonomy Id: 118163
Other names: P. sp. PCC 7327, Pleurocapsa minor OH-69-pm, Pleurocapsa sp. ATCC 29393, Pleurocapsa sp. PCC 7327
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