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secB protein (Alcaligenes faecalis) - STRING interaction network
"secB" - Protein-export protein SecB in Alcaligenes faecalis
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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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secBProtein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA (162 aa)    
Predicted Functional Partners:
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 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; Belongs to the SecA family (908 aa)
       
  0.976
secE
Protein 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 (126 aa)
   
 
  0.966
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 (441 aa)
     
  0.963
ffh
Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual componen [...] (474 aa)
         
  0.953
gpsA
Glycerol-3-phosphate dehydrogenase [NAD(P)+]; Derived by automated computational analysis using gene prediction method- Protein Homology (349 aa)
 
   
  0.945
yidC
Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (555 aa)
   
  0.936
JT27_15960
Preprotein translocase subunit SecG; Derived by automated computational analysis using gene prediction method- Protein Homology (135 aa)
       
  0.922
AFA_03245
Preprotein translocase subunit YajC; Derived by automated computational analysis using gene prediction method- Protein Homology (114 aa)
   
 
  0.919
grxC
Glutaredoxin; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (85 aa)
   
        0.845
secD
Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (623 aa)
   
     
  0.817
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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