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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ftsHCell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (669 aa)    
Predicted Functional Partners:
hptA/adkA
Bifunctional protein Hypoxanthine-guanine phosphoribosyltransferase / Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
 
 
 0.881
rpmA
Ribosomal protein L27 is part of the large ribosomal subunit (50S). It cross-links to the 23S rRNA and to the A and P site tRNAs. RpmA is essential for ribosome function, but its exact role is unclear; Belongs to the ribosomal protein L27p family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.859
rpsI
The ribosomal protein S9 is a part of the ribosomal small subunit (30S) that contributes to the structural integrity of the ribosome; Belongs to the ribosomal protein S9p/S16e family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.835
rplC
Ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
  
 
 0.827
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
   0.826
rplS
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.
  
 
 0.820
rpsP
Ribosomal protein S16 is one of the proteins from the 30S ribosomal subunit; In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity; Belongs to the ribosomal protein S16p family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.819
rplQ
Ribosomal protein L17 is one of the proteins from the 50S ribosomal subunit; Belongs to a ribosomal proteins L17b/YmL8 (yeast) family; Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.819
CAZ95766.1
The Band 7 protein is an integral membrane phosphoprotein of red blood cells thought to regulate cation conductance. Bacterial homologues are known, but their exact function is uncertain; Contains a N-terminal transmembrane helices; Localized in the cytoplasmic membrane; Family membership.
   
 0.813
CAZ98654.1
Conserved protein; Family membership.
   
 0.813
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.