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
rhlAAlpha/beta hydrolase fold family protein; 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 [...] (295 aa)    
Predicted Functional Partners:
Rhamnosyltransferase subunit b; Rhamnosyltransferase chain B; Glycosyltransferase family 28 N-terminal domain protein
Luxr family transcriptional regulator, quorum-sensing system regulator rhlr; 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)
Autoinducer synthetase family protein; Required for the synthesis of BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone) autoinducer molecules which bind to RhlR and thus acts in elastase biosynthesis regulation
Rhamnosyltran: rhamnosyltransferase family protein
Metallo-beta-lactamase superfamily protein; Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)- quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. Catalyzes the hydrolysis of the intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2- aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also hydrolyze other substrates such as S-ethyl-acetothioacetate and acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA and octanoy [...]
Amp-binding enzyme family protein; Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate
Pseudolysin; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase . Autocatalyses processing of its pro-peptide Processes the pro-peptide of pro-chitin-binding protein (cbpD) . Involved in the pathogenesis of P.aeruginosa infections
Luxr family transcriptional regulator, quorum-sensing system regulator lasr; Transcriptional activator of elastase structural gene (LasB). Binds to the PAI autoinducer
Lasa protease precursor; Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly- Gly-|-X substrates where X is Ala or Gly . Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases . Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in [...]
Atp-dependent rna helicase rhlb; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA
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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