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
yjbJ-2Transglycosylase. (206 aa)    
Predicted Functional Partners:
ssaT
Type III secretion protein.
 
  
 0.803
ALP40113.1
Hypothetical protein.
  
    0.767
ssaU
Secretion system apparatus protein SsaU.
       0.757
fliD
Flagellar hook protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
  
    0.489
ALP42948.1
Lytic transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family.
 
   
 0.489
ALP43436.1
LafB; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
  
    0.489
fliE
Flagellar hook-basal body protein.
  
  
 0.463
fliE-2
Lateral flagellar hook basal body protein, LfiE.
  
  
 0.463
yscN
ATP synthase.
  
    0.460
ALP41218.1
Lytic transglycosylase, glycoside hydrolase family 23; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family.
 
   
 0.432
Your Current Organism:
Aeromonas schubertii
NCBI taxonomy Id: 652
Other names: A. schubertii, ATCC 43700, Aeromonas hybridization group 12, CCUG 27820, CDC 2446-81, CECT 4240, CIP 103437, DSM 4882, Enteric Group 501, JCM 7373, LMG 9074, LMG:9074
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