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secE protein (Bifidobacterium adolescentis) - STRING interaction network
"secE" - Protein translocase subunit SecE in Bifidobacterium adolescentis
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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
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some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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secEProtein translocase subunit SecE; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation (75 aa)    
Predicted Functional Partners:
secG
annotation not available (85 aa)
 
  0.998
secY
Protein 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 (445 aa)
   
  0.998
secA
Protein 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 as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family (958 aa)
     
  0.978
rpmG
annotation not available (56 aa)
   
 
  0.974
nusG
Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination (274 aa)
   
   
  0.971
rpmJ
annotation not available (37 aa)
   
 
  0.971
rpmH
annotation not available (44 aa)
     
 
  0.970
rplV
50S ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome (119 aa)
 
 
  0.957
BADO_1742
annotation not available (344 aa)
 
  0.955
rpmI
annotation not available (64 aa)
   
      0.947
Your Current Organism:
Bifidobacterium adolescentis
NCBI taxonomy Id: 1680
Other names: AS 1.2190, ATCC 15703, B. adolescentis, BCRC 14606, Bifidobacterium adolescentis, CCRC 14606, CCUG 17359, CCUG 18363, CIP 64.59, DSM 20083, LMG 10502, NCAIM B.01822, NCTC 11814
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