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
hrpASimilar to E. coli helicase, ATP-dependent (AAC74495.1); Blastp hit to AAC74495.1 (1281 aa), 95% identity in aa 1 - 1280. (1300 aa)    
Predicted Functional Partners:
rpsA
30S ribosomal subunit protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
 
 0.789
rnd
RNase D; Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides; Belongs to the RNase D family.
  
 0.773
rpsD
30S ribosomal subunit protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
   
  0.763
gogB
Gifsy-1 prophage leucine-rich repeat protein.
    
 0.730
rpsK
30S ribosomal subunit protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
    
 0.670
ydcF
Putative inner membrane protein; Similar to E. coli orf, hypothetical protein (AAC74496.1); Blastp hit to AAC74496.1 (266 aa), 68% identity in aa 1 - 266.
  
    0.652
rtcA
RNA 3'-terminal phosphate cyclase (with b3419); Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
   
 
 0.630
rhlB
Putative helicase; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. Belongs to the DEAD box helicase family. RhlB subfamily.
  
 0.630
rpsE
30S ribosomal subunit protein S5; With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).
   
  0.621
srmB
ATP-dependent RNA helicase; DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity; Belongs to the DEAD box helicase family. SrmB subfamily.
 
 
 0.616
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.