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
EGZ50699.1PFAM: Outer membrane protein, OmpA/MotB, C-terminal; Rickettsia 17kDa surface antigen; KEGG: tgr:Tgr7_0120 OmpA/MotB domain protein. (221 aa)    
Predicted Functional Partners:
tolB
Protein tolB; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
  
 0.975
EGZ47858.1
KEGG: tgr:Tgr7_1168 outer membrane chaperone Skp (OmpH); PFAM: Outer membrane chaperone Skp (OmpH); SMART: Outer membrane chaperone Skp (OmpH); Belongs to the skp family.
  
 
 0.905
EGZ44815.1
Pyruvate dehydrogenase (NADP(+))., Pyruvate synthase; KEGG: hha:Hhal_0066 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; 4Fe-4S binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
  
   0.835
lolA
Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
  
 
 0.796
lolB
Outer-membrane lipoprotein lolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
   
 
 0.776
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
 
 0.775
rpsF
30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
  
   0.772
rpsL
Ribosomal protein S12; 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.
   
 
 0.770
EGZ50725.1
KEGG: tkm:TK90_0929 fagellar hook-basal body protein; TIGRFAM: Fagellar hook-basal body protein, FlgE/F/G; PFAM: Flagellar basal body FlaE; Flagellar basal body rod protein, N-terminal; Domain of unknown function DUF1078, C-terminal.
   
 0.769
rpsB
KEGG: tgr:Tgr7_1159 ribosomal protein S2; TIGRFAM: Ribosomal protein S2, bacteria/mitochondria/plastid; PFAM: Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family.
   
 
 0.768
Your Current Organism:
Thiorhodospira sibirica
NCBI taxonomy Id: 765914
Other names: T. sibirica ATCC 700588, Thiorhodospira sibirica A12, Thiorhodospira sibirica ATCC 700588, Thiorhodospira sibirica str. ATCC 700588, Thiorhodospira sibirica strain ATCC 700588
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.