STRINGSTRING
STRING protein interaction network
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rpmJ50S ribosomal protein L36; Smallest protein in the large subunit; similar to what is found with protein L31 and L33 several bacterial genomes contain paralogs which may be regulated by zinc; the protein from Thermus thermophilus has a zinc-binding motif and contains a bound zinc ion; the proteins in this group have the motif; Derived by automated computational analysis using gene prediction method: Protein Homology. (37 aa)    
Predicted Functional Partners:
rpsH
30S ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
  
 
 0.999
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
  
 
 0.999
rpmD
50S ribosomal protein L30; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.999
rpsM
30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family.
  
 
 0.999
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
  
 
 0.999
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
  
 
 0.998
rpmC
50S ribosomal protein L29; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uL29 family.
  
 
 0.998
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
 
 0.998
rplN
50S ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
  
 
 0.998
rplX
50S ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
  
 
 0.998
Your Current Organism:
Staphylococcus saprophyticus
NCBI taxonomy Id: 29385
Other names: ATCC 15305, BCRC 10786, CCM 883, CCRC 10786, CCRC:10786, CCUG 3706, CIP 76.125, DSM 20229, IAM 12452, JCM 2427, LMG 13350, LMG:13350, NBRC 102446, NCAIM B.01067, NCCB 73011, NCIB 8711, NCIB:8711, NCTC 7292, NRRL B-14751, S. saprophyticus, Staphylococcus sp. HAR3
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.