STRING protein interaction network
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 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
protein homology
Your Input:
Gene Fusion
lipCannotation not available (309 aa)    
Predicted Functional Partners:
Proteobacterial lipase chaperone family protein; May be involved in the folding of the extracellular lipase during its passage through the periplasm
Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol . It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity . It shows a marked specificity for the 1,3-oleyl residues of triolein
Prokaryotic diacylglycerol kinase family protein; Recycling of diacylglycerol produced during the turnover of membrane phospholipid
Outer membrane lipase/esterase; Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta- naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible
annotation not available
annotation not available
annotation not available
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives
annotation not available
Neisseria pilc beta-propeller domain protein; Involved in pilus assembly, twitching motility and adhesion to host cells. Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili . Stabilizes assembled pilus fibers likely by antagonizing retraction mediated by PilT. Calcium-binding and calcium release by PilY1 seem to be essential for twitching motility and for regulation of pilus retraction dynamics of PilT (By similarity)
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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