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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
AEB85087.1Transcriptional regulator, MerR family; Manually curated; PFAM: Transcription regulator MerR, DNA binding; HTH transcriptional regulator, MerR; KEGG: ajs:Ajs_2699 MerR family transcriptional regulator; SMART: HTH transcriptional regulator, MerR. (147 aa)    
Predicted Functional Partners:
AEB85065.1
Transcriptional regulator, MerR family; Manually curated; PFAM: Transcription regulator MerR, DNA binding; HTH transcriptional regulator, MerR; KEGG: ajs:Ajs_2675 MerR family transcriptional regulator; SMART: HTH transcriptional regulator, MerR.
  
     0.773
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
merA-2
Mercuric reductase; Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 
  
 0.506
AEB83830.1
TIGRFAM: Glutamine synthetase type I; KEGG: aav:Aave_1442 L-glutamine synthetase; PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp.
  
 
 0.461
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.
    
 
 0.458
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.
  
 
 0.453
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.
   
 
 0.441
merA
Mercuric reductase; Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 
   
 0.437
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.
    
 
 0.421
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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