STRINGSTRING
ACL43120.1 ACL43120.1 clpP clpP clpP-2 clpP-2 ACL44370.1 ACL44370.1 groL groL ACL44801.1 ACL44801.1 ACL44802.1 ACL44802.1 ACL45300.1 ACL45300.1 clpB clpB ACL46165.1 ACL46165.1 dnaK dnaK ACL46499.1 ACL46499.1 dnaK-2 dnaK-2 clpP-3 clpP-3 clpX clpX clpB-2 clpB-2 dnaJ dnaJ dnaK-3 dnaK-3 grpE grpE ACL47009.1 ACL47009.1 hrcA hrcA groL-2 groL-2 groS groS
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:
ACL43120.1PFAM: heat shock protein DnaJ domain protein; KEGG: ter:Tery_1240 heat shock protein DnaJ-like. (232 aa)
clpPEndopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (218 aa)
clpP-2Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (198 aa)
ACL44370.1ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. (656 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (553 aa)
ACL44801.1PFAM: Heat shock protein 70; KEGG: cya:CYA_0343 DnaK family protein. (520 aa)
ACL44802.1KEGG: cyb:CYB_1504 hypothetical protein. (213 aa)
ACL45300.1PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: amr:AM1_1111 heat shock protein DnaJ. (340 aa)
clpBATP-dependent chaperone ClpB; 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. (872 aa)
ACL46165.1PFAM: Heat shock protein 70; KEGG: amr:AM1_2057 DnaK family protein. (532 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (630 aa)
ACL46499.1PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: amr:AM1_5693 DnaJ-like protein. (333 aa)
dnaK-2Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (691 aa)
clpP-3ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (236 aa)
clpXATP-dependent Clp protease, 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. (447 aa)
clpB-2ATP-dependent chaperone ClpB; 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. (899 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 [...] (374 aa)
dnaK-3Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (643 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 [...] (246 aa)
ACL47009.1PFAM: UvrB/UvrC protein; AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; KEGG: tel:tll0307 ATP-dependent Clp protease regulatory subunit; Belongs to the ClpA/ClpB family. (825 aa)
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (364 aa)
groL-2Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (103 aa)
Your Current Organism:
Cyanothece sp. PCC7425
NCBI taxonomy Id: 395961
Other names: C. sp. PCC 7425, Cyanothece sp. ATCC 29141, Cyanothece sp. PCC 7425, Synechococcus sp. PCC 7425
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