STRINGSTRING
RSAG_02868 protein (Ruminococcus sp. 5139BFAA) - STRING interaction network
"RSAG_02868" - No annotation available in Ruminococcus sp. 5139BFAA
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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
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
RSAG_02868No annotation available (43 aa)    
Predicted Functional Partners:
infA
Translation initiation factor IF-1 ; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre- initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex (72 aa)
              0.859
RSAG_02866
Peptidase M ; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (251 aa)
              0.771
RSAG_02865
Adenylate kinase ; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (214 aa)
              0.671
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 (438 aa)
              0.512
rplO
50S ribosomal protein L15 ; Binds to the 23S rRNA (146 aa)
              0.512
Your Current Organism:
Ruminococcus sp. 5139BFAA
NCBI taxonomy Id: 457412
Other names: R. sp. 5_1_39BFAA, Ruminococcus 5_1_39BFAA, Ruminococcus sp. 5139BFAA, Ruminococcus sp. 5_1_39BFAA
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