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
chiAChitinase; Belongs to the glycosyl hydrolase 18 family (483 aa)    
Predicted Functional Partners:
Chitin binding domain protein; Binds chitin but does not hydrolyze it, has no detectable protease or staphylolytic activity
Beta-n-acetylhexosaminidase; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides (By similarity). Contributes to intrinsic fosfomycin resistance in P.aeruginosa
Phosphotransferase enzyme family protein; Sugar kinase that catalyzes the ATP-dependent phosphorylation of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1 hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P, respectively (By similarity). Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc . Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc
Putative phenazine-specific methyltransferase; 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)
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
Alkaline metalloproteinase precursor; Belongs to the peptidase M10B family
Pa-i galactophilic lectin; D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl- beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity
annotation not available
annotation not available
5-methylphenazine-1-carboxylate 1-monooxygenase; 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
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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