STRINGSTRING
ABI61528.1 ABI61528.1 dnaJ dnaJ dnaK dnaK grpE grpE htpG htpG ABI61275.1 ABI61275.1 ABI61339.1 ABI61339.1 secB secB ABI63167.1 ABI63167.1 ABI63094.1 ABI63094.1 groS groS groL groL ureE ureE clpB clpB ABI62649.1 ABI62649.1 ABI62359.1 ABI62359.1 ABI62226.1 ABI62226.1 tig tig clpX clpX ABI62115.1 ABI62115.1 ABI61839.1 ABI61839.1
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:
ABI61528.1Molecular chaperones (DnaJ family). (204 aa)
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 [...] (376 aa)
dnaKChaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (632 aa)
grpEgrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] (226 aa)
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (696 aa)
ABI61275.1Outer membrane protein. (259 aa)
ABI61339.1DnaJ-like protein djlA. (276 aa)
secBProtein translocase subunit secB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. (182 aa)
ABI63167.133 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. (317 aa)
ABI63094.1Peptidyl-prolyl cis-trans isomerase. (468 aa)
groS10 kDa chaperonin GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (101 aa)
groL60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa)
ureEUrease accessory protein ureE; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (176 aa)
clpBclpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. (865 aa)
ABI62649.1ATP-dependent clp protease ATP-binding subunit clpA; Belongs to the ClpA/ClpB family. (851 aa)
ABI62359.1Curved DNA-binding protein. (298 aa)
ABI62226.1Chaperone protein ecpD. (239 aa)
tigTrigger factor, ppiase; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. (444 aa)
clpXATP-dependent endopeptidase clp ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (420 aa)
ABI62115.1Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (186 aa)
ABI61839.1Hypothetical protein. (301 aa)
Your Current Organism:
Granulibacter bethesdensis
NCBI taxonomy Id: 391165
Other names: G. bethesdensis CGDNIH1, Granulibacter bethesdensis CGDNIH1, Granulibacter bethesdensis str. CGDNIH1, Granulibacter bethesdensis strain CGDNIH1
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.