Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ffhSignal recognition particle; 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. Belongs to the GTP-binding SRP family. SRP54 subfamily. (517 aa)    
Predicted Functional Partners:
ftsY
Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
 
0.995
rpsP
30S ribosomal protein S16; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bS16 family.
 
 
 0.958
yidC
Preprotein translocase YidC; Functions to insert inner membrane proteins into the IM in Escherichia coli; interacts with transmembrane segments; functions in both Sec-dependent and -independent membrane insertion; similar to Oxa1p in mitochondria; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.950
KUN40673.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.950
secE
Preprotein 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.
  
 
 0.935
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.930
KUN47565.1
Preprotein translocase, YajC subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.929
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
 
 
 
 0.928
secA-2
Preprotein 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.
    
 0.927
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
 
 0.926
Your Current Organism:
Streptomyces olivochromogenes
NCBI taxonomy Id: 1963
Other names: ATCC 25479, ATCC 3336, Actinomyces olivochromogenus, CBS 889.69, DSM 40451, IFO 13067, IFO 3178, IMET 40352, ISP 5451, JCM 4163, JCM 4500, KCTC 9064, NBRC 13067, NBRC 3178, NRRL-ISP 5451, S. olivochromogenes, Streptomyces olivichromogenes, Streptomyces olivochromogenus
Server load: medium (54%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.