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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
algKAlginate biosynthesis protein AlgK; May be involved in the polymerization of mannuronate to alginate. (484 aa)    
Predicted Functional Partners:
algX
Alginate biosynthesis protein AlgX; Plays two roles in the biosynthesis of the exopolysaccharide alginate: protects alginate from degradation as the polymer traverses the periplasm, and also plays a role in its O-acetylation. Probably has acetyltransferase activity in vivo (By similarity).
 
 0.999
algG
poly(beta-D-mannuronate) C5 epimerase; Catalyzes the epimerization of beta-D-mannuronate to alpha-L- guluronate during the synthesis of the linear polysaccharide alginate. In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE.
  
 
 0.999
algE
Alginate production protein AlgE; Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore.
  
 
 0.999
algL
Alginate lyase; Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space.
  
 
 0.998
alg8
Glycosyltransferase alg8; Possibly a processive enzyme that polymerizes GDP-mannuronic acid.
 
 0.997
alg44
Alginate biosynthesis protein Alg44; Required for alginate biosynthesis.
  
  
 0.993
algJ
Probable alginate O-acetylase AlgJ; Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity).
 
  
 0.990
algI
Probable alginate O-acetylase AlgI; Together with AlgJ and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity).
 
 
 0.964
algD
GDP-mannose 6-dehydrogenase; Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity).
  
  
 0.936
algF
Alginate biosynthesis protein AlgF; Together with AlgI and AlgJ, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity).
  
  
 0.935
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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