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
coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (162 aa)    
Predicted Functional Partners:
coaE
Dephospho-CoA kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family.
 
 
 0.974
dfp
Aldose 1-epimerase (pseudogene); Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
 
 
 0.958
coaX1
Transcriptional regulator; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family.
 
  
 0.932
coaX2
Transcriptional regulator; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family.
 
  
 0.931
fdx
Ferredoxin. Identical to Q47937 Ferredoxin from Francisella novicida. Similar to Q88AH4 Ferredoxin from pseudomonas syringae (83 aa). FASTA: opt: 431 Z-score: 563.2 E(): 1.8e-23 Smith-Waterman score: 431; 65.432 identity in 81 aa overlap.
  
  
 0.825
FTT_0579
Similar to AAP95950 HesB family protein from Haemophilus ducreyi (107 aa). FASTA: opt: 288 Z-score: 392.8 E(): 5.5e-14 Smith-Waterman score: 288; 41.121 identity in 107 aa overlap ORF ftt0579; Belongs to the HesB/IscA family.
  
    0.787
FTT_0580
Similar to Q83BY3 Hypothetical protein from Coxiella burnetii (180 aa). FASTA: opt: 593 Z-score: 750.6 E(): 6.4e-34 Smith-Waterman score: 593; 48.045 identity in 179 aa overlap ORF ftt0580.
       0.765
ribF
Riboflavin biosynthesis protein RibF; Similar to Q9CKF8 RibF from Pasteurella multocida (311 aa). FASTA: opt: 845 Z-score: 994.4 E(): 1.5e-47 Smith-Waterman score: 845; 44.481 identity in 308 aa overlap; Belongs to the ribF family.
 
   
 0.716
folK
Similar to Q821E2 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase/dihydropteroate synthase from Chlamydophila caviae (447 aa). FASTA: opt: 517 Z-score: 602.2 E(): 1.2e-25 Smith-Waterman score: 604; 30.664 identity in 437 aa overlap.
     
 0.695
ribA
Riboflavin biosynthesis protein ribA/GTP-cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the N-terminal section; belongs to the DHBP synthase family.
     
 0.686
Your Current Organism:
Francisella tularensis SCHUS4
NCBI taxonomy Id: 177416
Other names: F. tularensis subsp. tularensis SCHU S4, Francisella tularensis Biovar A str. SCHU S4, Francisella tularensis Biovar A str. Schu 4, Francisella tularensis subsp. tularensis SCHU S4, Francisella tularensis subsp. tularensis Schu 4, Francisella tularensis subsp. tularensis str. SCHU S4, Francisella tularensis subsp. tularensis strain SCHU S4
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.