close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
ybeDProtein lipolyation system protein YbeD; Belongs to the UPF0250 family. (88 aa)    
Predicted Functional Partners:
lipB
Lipoyl(octanoyl) transferase LipB; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
 
  
 0.991
lipA
Lipoic acid synthetase LipA; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
  
  
 0.967
dacA
D-alanyl-D-alanine carboxypeptidase DacA; Belongs to the peptidase S11 family.
 
    0.682
rraB
Ribonuclease E inhibitor 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.
  
    0.635
rseA
sigma-E factor negative regulatory protein RseA; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplas [...]
  
     0.611
bamD
Beta barrel protein translocation component BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
  
    0.607
metJ
Transcriptional repressor of methionine metabolism MetJ; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family.
  
    0.604
SO_2914
Protein of unknown function DUF412.
  
     0.561
lptE
OM lipoprotein component of lipopolysaccharide assembly complex chaperone LptE; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
 
    0.495
cpdA
Cyclic 3', 5'-adenosine monophosphate phosphodiesterase CpdA; Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes.
   
  
 0.493
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
Server load: low (30%) [HD]