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smpA protein (Yersinia pseudotuberculosis) - STRING interaction network
"smpA" - Outer membrane protein assembly factor BamE in Yersinia pseudotuberculosis
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query proteins and first shell of interactors
white nodes:
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
Others
textmining
co-expression
protein homology
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Score
smpAOuter 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 (113 aa)    
Predicted Functional Partners:
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. Constitutes, with BamA, the core component of the assembly machinery (243 aa)
   
 
  0.985
yaeT
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. Constitutes, with BamD, the core component of the assembly machinery (795 aa)
   
 
 
  0.980
nlpB
Outer membrane protein assembly factor BamC; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (352 aa)
   
 
 
  0.970
yfgL
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 (393 aa)
   
 
 
  0.960
recN
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA (553 aa)
   
        0.680
mreD
Rod shape-determining protein MreD; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (162 aa)
   
 
      0.678
lolB
Outer-membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein (207 aa)
   
   
  0.675
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) (202 aa)
   
     
  0.665
lpxH
UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (240 aa)
   
     
  0.614
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)
   
 
 
  0.612
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
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