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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
ACS21340.1Transcriptional regulator, MerR family; PFAM: Transcription regulator MerR DNA binding; regulatory protein MerR; SMART: regulatory protein MerR; KEGG: pna:Pnap_0453 MerR family transcriptional regulator. (132 aa)    
Predicted Functional Partners:
ACS19854.1
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: bav:BAV0873 curved DNA-binding protein.
  
 
 0.745
ACS21341.1
Cyclic nucleotide-binding protein; PFAM: beta-lactamase domain protein; KEGG: rfr:Rfer_3844 beta-lactamase-like.
 
  
 0.739
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 [...]
  
 
 0.697
aceK
(Isocitrate dehydrogenase (NADP(+))) kinase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
       0.689
ACS21339.1
Carbonate dehydratase; PFAM: carbonic anhydrase; KEGG: pol:Bpro_4189 carbonate dehydratase.
       0.689
ACS17371.1
PAS/PAC sensor hybrid histidine kinase; KEGG: scl:sce0929 two-component hybrid sensor and regulator; TIGRFAM: PAS sensor protein; PFAM: ATP-binding region ATPase domain protein; response regulator receiver; PAS fold-4 domain protein; PAS fold domain protein; histidine kinase A domain protein; SMART: ATP-binding region ATPase domain protein; response regulator receiver; histidine kinase A domain protein; PAC repeat-containing protein; PAS domain containing protein.
   
 
 0.608
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.606
rpoA
DNA-directed RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 0.599
rpoZ
DNA-directed RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
   
 
 0.595
rpoC
DNA-directed RNA polymerase, beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.587
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
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