STRINGSTRING
grpE grpE secB secB Nwi_0134 Nwi_0134 dnaK dnaK dnaJ dnaJ Nwi_0401 Nwi_0401 clpB clpB Nwi_0624 Nwi_0624 Nwi_0738 Nwi_0738 Nwi_0741 Nwi_0741 Nwi_1680 Nwi_1680 Nwi_1700 Nwi_1700 Nwi_1750 Nwi_1750 Nwi_1797 Nwi_1797 Nwi_1798 Nwi_1798 clpX clpX tig tig groL1 groL1 groS groS Nwi_2171 Nwi_2171 groS-2 groS-2 groL2 groL2 groS-3 groS-3 groL3 groL3 htpG htpG
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:
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 [...] (197 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. (159 aa)
Nwi_0134Hsp33 protein; 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. (334 aa)
dnaKHeat shock protein Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. (630 aa)
dnaJHeat shock 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, [...] (378 aa)
Nwi_0401Heat shock protein DnaJ. (232 aa)
clpBAAA ATPase; 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. (891 aa)
Nwi_0624Heat shock protein DnaJ. (316 aa)
Nwi_0738Conserved hypothetical protein. (174 aa)
Nwi_0741DSBA oxidoreductase. (222 aa)
Nwi_1680Conserved unknown protein. (314 aa)
Nwi_1700Heat shock protein DnaJ. (298 aa)
Nwi_1750DSBA oxidoreductase. (254 aa)
Nwi_1797Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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. (154 aa)
Nwi_1798Peptidyl-prolyl cis-trans isomerase, cyclophilin type; 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)
clpXClpX, ATPase regulatory subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (424 aa)
tigTrigger factor; 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. (453 aa)
groL1Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (104 aa)
Nwi_2171Peptidylprolyl isomerase, FKBP-type. (154 aa)
groS-2Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (105 aa)
groL2Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groS-3Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)
groL3Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (637 aa)
Your Current Organism:
Nitrobacter winogradskyi
NCBI taxonomy Id: 323098
Other names: N. winogradskyi Nb-255, Nitrobacter winogradskyi Nb-255, Nitrobacter winogradskyi str. Nb-255, Nitrobacter winogradskyi strain Nb-255
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