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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
AEB82480.1Transcriptional regulator, MerR family; TIGRFAM: Cu(I)-responsive transcriptional regulator; PFAM: Transcription regulator MerR, DNA binding; HTH transcriptional regulator, MerR; KEGG: dia:Dtpsy_0035 transcriptional regulator, MerR family; SMART: HTH transcriptional regulator, MerR. (145 aa)    
Predicted Functional Partners:
AEB82481.1
PFAM: Heavy metal transport/detoxification protein; KEGG: dia:Dtpsy_0036 heavy metal transport/detoxification protein.
  
  
 0.816
rpoD
RNA polymerase, sigma 70 subunit, RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
  
 
 0.716
AEB83089.1
KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 
 0.579
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 [...]
  
 
 0.579
AEB82482.1
TIGRFAM: ATPase, P-type, heavy metal translocating; ATPase, P type, cation/copper-transporter; ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter; KEGG: dia:Dtpsy_0037 heavy metal translocating P-type ATPase; PFAM: ATPase, P-type, ATPase-associated domain; Heavy metal transport/detoxification protein; Haloacid dehalogenase-like hydrolase.
  
  
 0.575
AEB82479.1
Hypothetical protein; KEGG: blt:Balat_0053 beta-galactosidase I.
       0.531
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.
  
 
 0.527
rpoZ
DNA-directed RNA polymerase subunit omega; 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.
   
 
 0.515
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.
    
 
 0.510
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.
    
 
 0.498
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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