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
ptrBProtease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. (686 aa)    
Predicted Functional Partners:
tesA
acyl-CoA thioesterase 1 and protease I and lysophospholipase L1; TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease. TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA. TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate. Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin [...]
      
 0.811
elaD
Protease, capable of cleaving an AMC-ubiquitin model substrate; Protease that can act as an efficient and specific deubiquitinating enzyme in vitro. Does not possess desumoylating and deneddylating activities. The physiological substrate is unknown.
      
 0.785
ptrA
Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin.
      
 0.784
sppA
Protease IV (signal peptide peptidase); Digests 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. Belongs to the peptidase S49 family.
  
   
 0.521
pqqL
Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease.
      
 0.503
prlC
Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4).
  
   
 0.501
yebE
DUF533 family inner membrane protein.
       0.461
dcp
Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family.
  
   
 0.451
rlpA
Septal ring protein, suppressor of prc, minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family.
  
   
 0.432
clpP
Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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.
   
  
 0.402
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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