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bamE protein (Methylobacter tundripaludum) - STRING interaction network
"bamE" - Outer membrane protein assembly factor BamE in Methylobacter tundripaludum
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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:
some 3D structure is known or predicted
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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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
bamEOuter membrane protein assembly factor BamE; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (187 aa)    
Predicted Functional Partners:
bamA
Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (793 aa)
   
 
  0.991
bamD
Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (279 aa)
   
  0.991
bamB
Outer membrane protein assembly factor BamB; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (416 aa)
   
 
  0.984
Mettu_3167
KEGG- mca-MCA0672 putative lipoprotein (214 aa)
       
  0.793
fur
PFAM- Ferric-uptake regulator; KEGG- mca-MCA2623 ferric uptake regulation protein; Belongs to the Fur family (139 aa)
 
     
  0.749
surA
Chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (434 aa)
   
 
 
  0.734
Mettu_3462
KEGG- hypothetical protein (666 aa)
       
  0.709
Mettu_2225
KEGG- msl-Msil_0411 hypothetical protein (475 aa)
       
  0.709
lptD
LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (985 aa)
   
 
 
  0.704
lolA
Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane) (196 aa)
   
     
  0.684
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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