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
hokDToxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within 2 minutes; causes collapse of the transmembrane potential and arrest of respiration (51 aa)    
Predicted Functional Partners:
hokA
Toxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration . Its toxic effect is probably neutralized by antisense antitoxin RNA SokA .
      
 0.877
relB
Antitoxin component of a type II toxin-antitoxin (TA) system. Counteracts the effect of cognate toxin RelE via direct protein-protein interaction, preventing RelE from entering the ribosome A site and thus inhibiting its endoribonuclease activity. An autorepressor of relBE operon transcription. 2 RelB dimers bind to 2 operator sequences; DNA- binding and repression is stronger when complexed with toxin/corepressor RelE by conditional cooperativity (PubMed:18501926, PubMed:22981948). Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in [...]
  
  
 0.829
hokE
Toxic component of a type I toxin-antitoxin (TA) system; if it expressed it could be neutralized by antisense antitoxin RNA SokE.
    
 
 0.792
relE
Toxic component of a type II toxin-antitoxin (TA) system . A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. In vitro mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl- tRNA in the P site as well as on free 30S subunits . In vivo cuts freque [...]
     
 0.708
dicC
This protein is a repressor of division inhibition gene dicB
      
 0.674
cspD
Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells
      
 0.640
mqsA
Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MqsR mRNA interferase toxin and neutralizes its endoribonuclease activity. Overexpression prevents MqsR-mediated cessation of cell growth and inhibition of cell proliferation. Initially reported to act as a cotranscription factor with MqsA . Following further experiments, the MqsR-MqsA complex does not bind DNA and all reported data are actually due to a small fraction of free MqsA alone binding DNA. Addition of MqsR to a preformed MqsA-promoter DNA complex causes dissociation of the MqsA-D [...]
      
 0.640
mqsR
Toxic component of a type II toxin-antitoxin (TA) system. Plays a significant role in the control of biofilm formation and induction of persister cells in the presence of antibiotics. An mRNA interferase which has been reported to be translation-independent . It has also been reported to be translation-dependent . Cleavage has been reported to occur on either side of G in the sequence GCU . Also reported to cleave after C in GC(A/U) sequences . There are only 14 genes in E.coli W3110 (and probably also MG1655) that do not have a GCU sequence and thus are resistant to the mRNA interfera [...]
      
 0.619
xapA
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine. ECO:0000269|PubMed:3042752, ECO:0000269|PubMed:7007808,
      
 0.609
hokB
Toxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration . Expression leads to membrane depolarization; when protein levels are high enough depolarization probably leads to lowered metabolic activity which in turn induces some cells to enter the persistent state in which they transiently survive antibiotic exposure. Its toxic effect is probably neutralized by antisense antitoxin RNA SokB, which is encoded in trans on the opposite DNA strand
      
 0.609
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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