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
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
azo2154Conserved hypothetical secreted protein. 33% similarity to TrEMBL Q8XQF8 PROBABLE SIGNAL PEPTIDE PROTEIN [RS05314] [Ralstonia solanacearum (Pseudomonas solanacearum)]. No domains predicted. Signal P reporting signal peptide present. No TMH reported being present; Conserved hypothetical protein. (156 aa)    
Predicted Functional Partners:
azo2155
Conserved hypothetical secreted protein. Homology to rsc1270 of R. solanacearum of 44% (trembl|Q8XQF7(SRS)). no domains predicted .signal peptide present. no TMHs; Conserved hypothetical protein.
 
     0.952
azo0358
Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases).
  
 0.851
azo2156
TonB-dependent outer membrane receptor involved in the first step of iron internalization and metabolism. A short conserved region so called the tonB-box is present in the sequence. This domain is involved in the interaction of the receptor with the TonB protein. Similar to a E. coli iron(III) dicitrate transport protein fecA precursor. InterPro: TonB-dependent receptor protein arcC: carbamate kinase; Function unclear.
 
     0.823
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.
    
 0.804
ppiA
Probable peptidyl-prolyl cis-trans isomerase A; 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.
    
 0.804
cutA2
Putative protein disulfide-isomerase; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily.
 
 
 0.791
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.788
hscA
Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
   
 0.788
azo3626
Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership.
   
 0.788
dnaJ1
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 [...]
    
 0.787
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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