STRINGSTRING
dnaJ dnaJ dnaK dnaK AGB03550.1 AGB03550.1 AGB03777.1 AGB03777.1 AGB03894.1 AGB03894.1 AGB01369.1 AGB01369.1 AGB01782.1 AGB01782.1 AGB02125.1 AGB02125.1 pfdA pfdA pfdB pfdB AGB02230.1 AGB02230.1 AGB02649.1 AGB02649.1 AGB03782.1 AGB03782.1 AGB02656.1 AGB02656.1
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 [...] (377 aa)
dnaKChaperone protein DnaK; Acts as a chaperone. (622 aa)
AGB03550.1Molecular chaperone; PFAM: MreB/Mbl protein; Belongs to the heat shock protein 70 family. (533 aa)
AGB03777.1Molecular chaperone (small heat shock protein); PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family. (160 aa)
AGB03894.1PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. (551 aa)
AGB01369.1PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. (532 aa)
AGB01782.1Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. (550 aa)
AGB02125.1Molecular chaperone (small heat shock protein); PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family. (157 aa)
pfdAPrefoldin alpha subunit/subunit 5; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. (143 aa)
pfdBPrefoldin, beta subunit, archaeal; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. (120 aa)
AGB02230.1Hypothetical protein. (139 aa)
AGB02649.1Hypothetical protein. (146 aa)
AGB03782.1Hypothetical protein. (90 aa)
AGB02656.1RecJ-like exonuclease with DnaJ-type Zn-finger domain; PFAM: DHH family; S1 RNA binding domain; OB-fold nucleic acid binding domain. (616 aa)
Your Current Organism:
Methanoregula formicica
NCBI taxonomy Id: 593750
Other names: M. formicica SMSP, Methanomicrobiales archaeon SMSP, Methanoregula formicica SMSP, Methanoregula formicica str. SMSP, Methanoregula formicica strain SMSP
Server load: low (24%) [HD]