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
SFJ24052.1DivIVA domain-containing protein. (207 aa)    
Predicted Functional Partners:
SFJ24021.1
NAD(P)H-flavin reductase; Belongs to the globin family.
 
     0.840
SFJ24074.1
Hemoglobin.
 
     0.834
SFI68914.1
Membrane carboxypeptidase (penicillin-binding protein).
   
 
 0.761
SFJ52949.1
Membrane carboxypeptidase (penicillin-binding protein).
   
 
 0.761
SFJ78133.1
Membrane carboxypeptidase (penicillin-binding protein).
   
 
 0.761
SFK57856.1
Membrane carboxypeptidase (penicillin-binding protein).
   
 
 0.761
SFK86253.1
Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
  
  
 0.584
SFJ55863.1
Serine/threonine protein kinase.
  
 
 0.552
SFK35814.1
Serine/threonine protein kinase.
  
 
 0.552
sepF
Cell division inhibitor SepF; Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
  
  
 0.539
Your Current Organism:
Amycolatopsis sacchari
NCBI taxonomy Id: 115433
Other names: A. sacchari, Amycolatopsis sacchari Goodfellow et al. 2001, CIP 107029, DSM 44468, JCM 11272, KCTC 9863, NBRC 100339
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