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
sppADigests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane. (618 aa)    
Predicted Functional Partners:
ydjA
Belongs to the nitroreductase family
     
 0.772
ansA
Belongs to the asparaginase 1 family
 
    0.764
lepB
Signal peptidase I; Enzyme; Protein, peptide secretion; Belongs to the peptidase S26 family
  
   
 0.755
pncA
Catalyzes the deamidation of nicotinamide (NAM) into nicotinate . Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide
  
  
 0.689
trpC
Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain
     
 0.664
clpP
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE . ECO:0000269|PubMed:12941278, ECO:0000269|PubMed:15371343,
      
 0.620
ptrB
Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues
  
   
 0.564
yshB
annotation not available
      
 0.563
glpG
Rhomboid-type serine protease that catalyzes intramembrane proteolysis
  
  
 0.538
rseP
A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lp [...]
 
 
 
 0.536
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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