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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lecBannotation not available (115 aa)    
Predicted Functional Partners:
lecA
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
   
  
 0.968
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,
   
  
 0.750
rpoS
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response.
   
  
 0.726
DR97_4499
DUF1302 domain-containing protein
      
 0.681
rhlB
DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA.
      
 0.674
chiA
Belongs to the glycosyl hydrolase 18 family.
      
 0.670
phzH
Potential phenazine-modifying enzyme; asn_synth_AEB: asparagine synthase
   
  
 0.668
oprF
Has porin activity, forming small water-filled channels. Also has a structural role in determining cell shape and ability to grow in low-osmolarity medium
      
 0.640
lap
A secreted aminopeptidase. Acts on free N-terminal amino groups with a very strong preference for Leu- followed by Met- and Ala-, and no activity on Glu- or Gly- peptides (an exhaustive analysis was not performed). Both the AP56 and AP28 forms have activity.
   
    0.584
lasA
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 a given catalytic cycle, [...]
      
 0.576
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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