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
SHI95700.1Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape. (271 aa)    
Predicted Functional Partners:
SHI95716.1
Rod shape-determining protein MreB.
 
 
 0.991
SHI95655.1
Penicillin-binding protein 2.
 
 
 0.970
SHI95632.1
Rod shape determining protein RodA; Belongs to the SEDS family.
 
  
 0.921
SHI95676.1
Hypothetical protein.
  
    0.821
SHJ05334.1
Cell division protein FtsI (penicillin-binding protein 3).
 
 
 0.757
SHI35441.1
DNA repair protein RadC; Belongs to the UPF0758 family.
  
  
 0.738
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
       0.680
SHI70608.1
Protein of unknown function.
  
 
 0.644
SHI68779.1
Penicillin-binding protein 1A.
  
 
 
 0.594
SHI57368.1
Septum formation protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
  
  
 0.574
Your Current Organism:
Arenitalea lutea
NCBI taxonomy Id: 1178825
Other names: A. lutea, Arenitalea lutea Zhang et al. 2013, CGMCC 1.12213, Flavobacteriaceae bacterium P7-3-5, KACC 16457, strain P7-3-5
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.