STRINGSTRING
clpX protein (Janibacter sp. HTCC2649) - STRING interaction network
"clpX" - ATP-dependent Clp protease ATP-binding subunit ClpX in Janibacter sp. HTCC2649
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:
some 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 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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
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 (424 aa)    
Predicted Functional Partners:
JNB_05869
Endopeptidase 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 (219 aa)
  0.997
JNB_05874
Endopeptidase 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 (206 aa)
  0.997
ftsZ
Cell division protein FtsZ ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (422 aa)
 
 
 
  0.937
grpE
HSP-70 cofactor ; 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- depend [...] (215 aa)
   
 
  0.774
clpB
Chaperone protein 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 (855 aa)
   
 
  0.767
groS
Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
   
 
  0.738
JNB_17488
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (541 aa)
 
 
  0.735
JNB_16609
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
 
 
  0.726
dnaK
Heat shock protein 70 ; Acts as a chaperone (636 aa)
   
 
  0.716
JNB_03675
30S ribosomal protein S1 (502 aa)
 
     
  0.711
Your Current Organism:
Janibacter sp. HTCC2649
NCBI taxonomy Id: 313589
Other names: J. sp. HTCC2649, Janibacter, Janibacter HTCC2649, Janibacter sp. HTCC2649
Server load: low (14%) [HD]