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UMN179_00107 protein (Gallibacterium anatis) - STRING interaction network
"UMN179_00107" - 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase in Gallibacterium anatis
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second shell of interactors
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proteins of unknown 3D structure
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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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[Homology]
Score
UMN179_001073-deoxy-D-manno-octulosonate 8-phosphate phosphatase (186 aa)    
Predicted Functional Partners:
kdsA
2-dehydro-3-deoxyphosphooctonate aldolase (284 aa)
   
  0.998
kdsB
3-deoxy-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria (258 aa)
 
  0.996
UMN179_00106
D-arabinose 5-phosphate isomerase (311 aa)
 
 
  0.995
UMN179_01504
3-deoxy-D-manno-octulosonic-acid transferase (424 aa)
 
 
  0.879
lpxB
lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (396 aa)
 
 
  0.676
lpxK
Tetraacyldisaccharide 4’-kinase; Transfers the gamma-phosphate of ATP to the 4’-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1- P) to form tetraacyldisaccharide 1,4’-bis-phosphate (lipid IVA) (325 aa)
 
     
  0.658
lptC
Hypothetical protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA (228 aa)
   
   
  0.595
UMN179_00926
Cyclic beta-1,2-glucan ABc transporter (613 aa)
         
  0.586
msbA
Lipid transporter ATP-binding/permease; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (582 aa)
         
  0.586
UMN179_02422
Inosine 5’-monophosphate dehydrogenase (523 aa)
 
 
  0.577
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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