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
yhbYHypothetical protein yhbY; Escherichia coli K-12 ortholog: b3180; Escherichia coli O157:H7 ortholog: z4542. (97 aa)    
Predicted Functional Partners:
ybeN
Nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
  
  
 0.764
yjgA
Hypothetical protein yjgA; X96 protein; Escherichia coli K-12 ortholog: b4234; Escherichia coli O157:H7 ortholog: z5844; Belongs to the UPF0307 family.
  
   
 0.760
ftsJ
Ribosomal RNA large subunit methyltransferase J; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
  
  
 0.632
ybeB
Hypothetical protein ybeB; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
  
 0.550
barA
Sensor protein barA; Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay (By similarity).
     
 0.481
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
     
 0.456
infA
Translation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
   
    0.435
ybcJ
Hypothetical protein ybcJ; Escherichia coli K-12 ortholog: b0528; Escherichia coli O157:H7 ortholog: z0683.
   
  
 0.434
evgS
Sensor protein evgS precursor; Escherichia coli K-12 ortholog: b2370; Escherichia coli O157:H7 ortholog: z3632.
     
 0.430
yggJ
Hypothetical protein yggJ; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity); Belongs to the RNA methyltransferase RsmE family.
 
  
 0.419
Your Current Organism:
Escherichia coli CFT073
NCBI taxonomy Id: 199310
Other names: E. coli CFT073, Escherichia coli str. CFT073, Escherichia coli strain CFT073
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.