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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
clpAATP-dependent clp protease ATP-binding subunit (clpA); Psort: bacterial cytoplasm --- Certainty= 0.164(Affirmative); COG0542 ClpA ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. (781 aa)    
Predicted Functional Partners:
clpP
ATP-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.
   
 
 0.945
hscA
Heat shock protein (hscA); Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 
 0.910
dnaK
DNAK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.910
grpE
GrpE protein (grpE); 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-depe [...]
  
 
 0.833
dnaJ
DNAJ 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, DnaK [...]
  
 
 0.761
AMF_867
Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.582(Affirmative).
  
 
 0.740
htpG
Heat shock protein (htpG); Molecular chaperone. Has ATPase activity.
  
 
 0.703
ftsJ
Cell division protein (ftsJ); Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
   
   0.669
groEL
60 kD chaperonin (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.666
lon
ATP-dependent protease LA (lon); ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 
 0.648
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
Server load: low (18%) [HD]