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
ADW17448.1KEGG: ppd:Ppro_0194 hypothetical protein; SPTR: Putative uncharacterized protein. (246 aa)    
Predicted Functional Partners:
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 0.975
rpoA
DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 0.972
rplK
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
  
 
 0.968
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
   0.950
rpsJ
SSU ribosomal protein S10P; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
  
 
 0.942
rpsG
SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
  
 
 0.941
ADW16986.1
COGs: COG0522 Ribosomal protein S4 and related protein; InterPro IPR001912: IPR002942: IPR005709: IPR018079; KEGG: dps:DP1151 30S ribosomal protein S4; PFAM: ribosomal protein S4; RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; SPTR: 30S ribosomal protein S4; TIGRFAM: ribosomal protein S4; PFAM: Ribosomal protein S4/S9 N-terminal domain; S4 domain; TIGRFAM: ribosomal protein S4, bacterial/organelle type.
   
   0.933
nusG
Transcription antitermination protein nusG; Participates in transcription elongation, termination and antitermination.
  
 
 0.921
rpsB
COGs: COG0052 Ribosomal protein S2; InterPro IPR001865: IPR005706: IPR017871: IPR018130; KEGG: dak:DaAHT2_0967 ribosomal protein S2; PFAM: ribosomal protein S2; SPTR: Ribosomal protein S2; TIGRFAM: ribosomal protein S2; PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein S2, bacterial type; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.913
rpsL
SSU ribosomal protein S12P; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
  
 
 0.906
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.