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bamD protein (Xanthomonas campestris campestris) - STRING interaction network
"bamD" - Outer membrane protein assembly factor BamD in Xanthomonas campestris campestris
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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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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
bamDOuter 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 (293 aa)    
Predicted Functional Partners:
oma
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 (818 aa)
 
 
  0.989
bamE
Outer 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 (131 aa)
   
 
  0.976
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 (406 aa)
 
 
  0.956
XCC1742
annotation not available (172 aa)
   
 
  0.869
imp
LPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (809 aa)
 
 
  0.862
secB
Protein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA (170 aa)
   
     
  0.831
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) (209 aa)
   
 
  0.800
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta’ subunit thereby facilitating its interaction with the beta and alpha subunits (99 aa)
 
      0.783
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 (463 aa)
   
 
  0.754
rluD
Ribosomal large subunit pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA (259 aa)
   
        0.733
Your Current Organism:
Xanthomonas campestris campestris
NCBI taxonomy Id: 340
Other names: X. campestris pv. campestris, Xanthomonas campestris, Xanthomonas campestris (pv. campestris), Xanthomonas campestris campestris, Xanthomonas campestris pv. campestris
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