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
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Co-expression
Experiments
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[Homology]
Score
SPO3904Heat shock protein; 'initially identified as a pseudogene, expression verified by proteomics'; Belongs to the small heat shock protein (HSP20) family. (139 aa)    
Predicted Functional Partners:
clpB
ATP-dependent Clp protease, ATP-binding subunit 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.
 
 
 0.748
clpA
ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family.
 
 
 0.737
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.600
SPO2991
Identified by match to protein family HMM PF00881.
  
    0.559
SPO3857
Hypothetical protein; Identified by similarity to GB:BAA34646.1; match to protein family HMM PF04543.
   
    0.533
dtd
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
       0.530
grpE
Co-chaperone 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-depend [...]
  
 
 0.524
SPO2993
Identified by match to protein family HMM PF05161.
       0.518
SPO0092
Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928.
  
 
 0.500
groEL
Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
 0.460
Your Current Organism:
Ruegeria pomeroyi
NCBI taxonomy Id: 246200
Other names: R. pomeroyi DSS-3, Ruegeria pomeroyi DSS-3, Ruegeria pomeroyi str. DSS-3, Ruegeria pomeroyi strain DSS-3, Silicibacter pomeroyi DSS-3
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