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:
some 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
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[Homology]
Score
phzA1Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzA1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth (162 aa)    
Predicted Functional Partners:
phzF1
Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.
 
 
 0.988
phzG1
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
  
 
 0.986
DR97_5945
annotation not available
 
  
 0.920
phzD1
Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzD1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth . Catalyzes the hydrolysis of the vinyl ether functional group of 2-amino-2-deoxyisochorismate (ADIC), yielding pyruvate and trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) . Also able to act on isochorismate, chorismate and 4-amino-4-deoxychorismate (ADC) as substrates
 
    0.915
phzS
Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Catalyzes the oxidative decarboxylation of 5-methylphenazine-1-carboxylate (5-methyl- PCA) to pyocyanine. Can also act on phenazine-1-carboxylate (PCA), converting it into 1-hydroxyphenazine (1-HP). However, PCA is a poor substrate
  
  
 0.907
phzM
Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Converts phenazine-1-carboxylate (PCA) to 5-methylphenazine-1-carboxylate (5- methyl-PCA)
  
   
 0.872
sdiA
Necessary for transcriptional activation of the rhlAB genes encoding the rhamnosyltransferase. It also functions as a transcriptional activator of elastase structural gene (lasB). Binds to autoinducer molecules BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone)
 
   
 0.868
lasB
Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase . Autocatalyses processing of its pro-peptide (PubMed:9642203, PubMed:1744034). Processes the pro-peptide of pro-chitin-binding protein (cbpD) . Involved in the pathogenesis of P.aeruginosa infections. ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:1744034,
  
   
 0.861
phzB1
Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzB1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth
 
  
0.859
rhlA
Required for rhamnolipid surfactant production . Supplies the acyl moieties for rhamnolipid biosynthesis by competing with the enzymes of the type II fatty acid synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein (ACP) pathway intermediates. Catalyzes the formation of one molecule of beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta- hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid component of rhamnolipid. In vitro results establish that RhlA is highly selective for 10-carbon acyl-ACP intermediates and thus functions as the mo [...]
      
 0.849
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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