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
DR97_2259annotation not available (310 aa)    
Predicted Functional Partners:
putA
Oxidizes proline to glutamate for use as a carbon and nitrogen source
    
 0.939
speC
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
  
 
 0.915
proC
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline
    
 0.910
pip
Belongs to the peptidase S33 family.
     
  0.900
LivF
Belongs to the ABC transporter superfamily.
  
  
 0.668
BraE
Belongs to the binding-protein-dependent transport system permease family
  
    0.645
BraD
Belongs to the binding-protein-dependent transport system permease family
     
 0.635
BraF
annotation not available
       0.634
DR97_668
Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy- L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L- proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5- carboxylate (P5C) as substrate
 
   
 0.525
DR97_682
Probably catalyzes the dehydration of trans-3-hydroxy-L- proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source . Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor proline racemase activity .
 
   
 0.489
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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