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:
a 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pqiAParaquat-inducible protein A; Derived by automated computational analysis using gene prediction method: Protein Homology. (424 aa)    
Predicted Functional Partners:
KKF34925.1
Paraquat-inducible protein B; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.978
KKF34927.1
ABC transporter ATPase; Uup; in Escherichia coli this cytoplasmic protein was shown to contain ATPase activity; mutations in this gene affect RecA-independent excision of transposons and affects Mu bacteriophage growth; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.869
rlmL
23S rRNA methyltransferase; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Belongs to the methyltransferase superfamily. RlmKL family.
       0.869
lipB
Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
   
    0.572
Your Current Organism:
Erwinia tracheiphila
NCBI taxonomy Id: 65700
Other names: ATCC 33245, Bacillus tracheiphilus, Bacterium tracheiphilus, CFBP 2355, CIP 105205, DSM 21139, E. tracheiphila, Erwinia amylovora var. tracheiphila, ICMP 5845, LMG 2707, LMG 2906, LMG:2707, LMG:2906, NCPPB 2452
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