STRINGSTRING
UMN179_00070 protein (Gallibacterium anatis) - STRING interaction network
"UMN179_00070" - Outer membrane protein A in Gallibacterium anatis
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
UMN179_00070Outer membrane protein A (361 aa)    
Predicted Functional Partners:
UMN179_01876
Periplasmic chaperone (175 aa)
     
 
  0.888
tolB
Translocation protein TolB; Involved in the TonB-independent uptake of proteins (432 aa)
 
 
  0.880
UMN179_00071
Hypothetical protein (105 aa)
              0.859
UMN179_02049
Peptidoglycan-associated outer membrane lipoprotein (150 aa)
   
 
0.814
bamA
Outer membrane protein assembly factor YaeT; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (803 aa)
   
 
  0.814
secA
Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (928 aa)
       
 
  0.799
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (441 aa)
     
 
  0.788
UMN179_00585
Serine endoprotease (462 aa)
     
 
  0.698
UMN179_00177
Serine endoprotease (346 aa)
     
 
  0.698
UMN179_02166
Outer membrane phosphoporin protein E (381 aa)
     
  0.692
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
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