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
CCH87930.1Protein of unknown function; No homology to any previously reported sequences. (664 aa)    
Predicted Functional Partners:
pyrK
Dihydroorotate dehydrogenase electron transfer subunit; Function of strongly homologous gene; enzyme.
   
 0.861
CCH87931.1
Lysine exporter protein (LYSE/YGGA); Function of strongly homologous gene; transporter.
       0.773
dnaJ
Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...]
    
 
 0.727
dnaJ-2
Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...]
    
 
 0.727
CCH90928.1
Protein of unknown function; No homology to any previously reported sequences.
  
    0.726
ppiB
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
 
 0.720
ppiB-2
Putative peptidyl-prolyl cis-trans isomerase B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
    
 
 0.720
CCH85625.1
Exported protein of unknown function; No homology to any previously reported sequences.
  
   
 0.712
CCH87830.1
Exported protein of unknown function; No homology to any previously reported sequences.
  
   
 0.683
CCH85524.1
Homologs of previously reported genes of unknown function.
  
     0.658
Your Current Organism:
Modestobacter marinus
NCBI taxonomy Id: 477641
Other names: CGMCC 4.5581, DSM 45201, M. marinus, Modestobacter marinus Xiao et al. 2011, Modestobacter sp. 42H12-1, strain 42H12-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.