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
ymdBDeacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate . Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation . Overexpression inhibits biofilm formation via an RNase III-independent pathway. This inhibition is RpoS-dependent . Overexpression also results in increased susceptibility to apramycin (PubMed:28034758, PubMed:28582517). ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:24267348, ECO:0000269|PubMed:26481419, ECO:0000269|PubMed:28034758, (177 aa)    
Predicted Functional Partners:
clsC
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE)
  
  
 0.991
ymdA
annotation not available
     
 0.935
rraB
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome
      
 0.806
rarA
DNA-dependent ATPase that plays important roles in cellular responses to stalled DNA replication processes.
 
    0.773
rraA
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. ECO:0000269|PubMed:16771842, ECO:0000269|PubMed:18510556,
   
  
 0.771
cmk
ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.
 
    0.762
clsB
Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate. Rule:MF_01917, ECO:0000269|PubMed:10634942,
      
 0.733
pgaB
Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D- glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin.
     
 0.646
clsA
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Rule:MF_00190, ECO:0000269|PubMed:1663113,
      
 0.560
rnc
Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing substrate re [...]
    
 
 0.529
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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