STRINGSTRING
STRING protein interaction network
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ACZ08083.1KEGG: hypothetical protein. (926 aa)    
Predicted Functional Partners:
ACZ08076.1
PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: wbm:Wbm0785 DnaJ-like molecular chaperone.
  
 0.877
grpE
GrpE 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 [...]
  
 
 0.863
clpB
ATP-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.
  
 
 0.860
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.854
dnaJ
Chaperone 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 [...]
  
 0.833
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.812
ACZ07154.1
TIGRFAM: SUF system FeS assembly protein, NifU family; PFAM: nitrogen-fixing NifU domain protein; KEGG: lpc:LPC_2694 nitrogen fixation protein (Fe-S cluster formation) NifU.
  
 0.811
ACZ07497.1
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: pca:Pcar_1604 NADP-reducing hydrogenase chain C.
  
 0.786
ACZ10434.1
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: ppd:Ppro_3516 NADH dehydrogenase (quinone).
  
 0.786
ACZ08079.1
SMART: protein phosphatase 2C domain protein; KEGG: rsq:Rsph17025_3425 hypothetical protein.
  
 
 0.757
Your Current Organism:
Sebaldella termitidis
NCBI taxonomy Id: 526218
Other names: S. termitidis ATCC 33386, Sebaldella termitidis ATCC 33386, Sebaldella termitidis NCTC 11300, Sebaldella termitidis str. ATCC 33386, Sebaldella termitidis strain ATCC 33386
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