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UMN179_01425 protein (Gallibacterium anatis) - STRING interaction network
"UMN179_01425" - Hypothetical protein 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
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Experiments
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[Homology]
Score
UMN179_01425Hypothetical protein (315 aa)    
Predicted Functional Partners:
obg
GTPase ObgE; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control (388 aa)
   
        0.867
UMN179_00926
Cyclic beta-1,2-glucan ABc transporter (613 aa)
   
      0.632
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)
   
      0.632
UMN179_00250
Paraquat-inducible protein B (885 aa)
   
          0.482
UMN179_02178
Putative permease YjgP/YjgQ family (356 aa)
 
        0.468
rpmG
50S ribosomal protein L33 (56 aa)
              0.467
rpmB
50S ribosomal protein L28 (78 aa)
   
        0.465
UMN179_01873
CDP-diglyceride synthase (288 aa)
     
      0.463
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)
     
      0.448
UMN179_02043
Cyd operon protein YbgE (95 aa)
   
          0.434
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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