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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
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htpX-2Putative heat shock protein (htpX); Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the peptidase M48B family. (324 aa)    
Predicted Functional Partners:
ftsH
Metalloprotease (cell division protein) FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
  
 0.750
grpE
Possible heat shock protein (HSP-70 COFACTOR), 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 c [...]
  
  
 0.586
RPA0786
Putative Adenylate/Guanylate cyclase.
       0.571
trx
Possible thioredoxin; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
  
  
 0.564
clpB
Endopeptidase Clp: ATP-binding subunit B, 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the C [...]
  
  
 0.538
cysN
Putative CysN/CysC bifunctional enzyme, ATP-sulfurylase large subunit and adenylyl sulfate kinase; Catalyzes the synthesis of activated sulfate.
   
    0.503
clpA
Endopeptidase Clp: ATP-binding chain A; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the ClpA/ClpB family.
  
  
 0.503
dnaJ
Heat shock protein DnaJ (40); 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 D [...]
  
 
 0.499
RPA0785
Possible cytochrome P450 family proteins; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
  
   0.498
lon
ATP-dependent protease 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.
   
 
 0.498
Your Current Organism:
Rhodopseudomonas palustris CGA009
NCBI taxonomy Id: 258594
Other names: R. palustris CGA009, Rhodopseudomonas palustris str. CGA009, Rhodopseudomonas palustris strain CGA009
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