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secF protein (Xanthomonas campestris campestris) - STRING interaction network
"secF" - Protein-export membrane protein SecF in Xanthomonas campestris campestris
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query proteins and first shell of interactors
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second shell of interactors
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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secFProtein-export membrane protein SecF; 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 (322 aa)    
Predicted Functional Partners:
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 (622 aa)
0.999
queA
S-adenosylmethionine-tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA) (356 aa)
     
  0.895
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...] (381 aa)
 
   
  0.874
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 (455 aa)
   
 
  0.869
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 (136 aa)
     
 
  0.841
yajC
Preprotein translocase subunit YajC (117 aa)
 
   
  0.819
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 (575 aa)
   
 
  0.804
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family (364 aa)
         
  0.685
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis (186 aa)
 
        0.591
tatC
Sec-independent protein translocase protein TatC; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides (245 aa)
 
   
  0.572
Your Current Organism:
Xanthomonas campestris campestris
NCBI taxonomy Id: 340
Other names: X. campestris pv. campestris, Xanthomonas campestris, Xanthomonas campestris (pv. campestris), Xanthomonas campestris campestris, Xanthomonas campestris pv. campestris
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