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
PSM36_3338MoxR-like ATPase; High confidence in function and specificity. (331 aa)    
Predicted Functional Partners:
PSM36_3339
Hypothetical protein; High confidence in function and specificity.
  
 0.957
PSM36_3341
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant trans [...]
 
  
 0.932
PSM36_3342
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant trans [...]
 
  
 0.874
PSM36_3340
Hypothetical protein; High confidence in function and specificity.
 
    0.793
PSM36_3343
Hypothetical protein; High confidence in function and specificity.
 
   
 0.597
lipB
Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
       0.550
PSM36_3344
Oxygen tolerance; This family of proteins carries up to three membrane spanning regions and is involved in tolerance to oxygen in in Bacteroides spp; High confidence in function and specificity.
 
   
 0.547
PSM36_3345
Putative membrane protein.
 
    0.435
maeB
Bifunctional malic enzyme oxidoreductase/phosphotransacetylase; (S)-malate + NADP(+) <=> pyruvate + CO(2) + NADPH, Oxaloacetate <=> pyruvate + CO(2); High confidence in function and specificity.
  
    0.420
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
       0.415
Your Current Organism:
Proteiniphilum saccharofermentans
NCBI taxonomy Id: 1642647
Other names: CECT 8610, DSM 28694, LMG 28299, LMG:28299, P. saccharofermentans, Proteiniphilum saccharofermentans Hahnke et al. 2016, Proteiniphilum sp. M3/6, strain M3/6
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