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
bamDOuter membrane protein assembly factor BamD precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (251 aa)    
Predicted Functional Partners:
bamA
Outer membrane protein assembly factor BamA precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
 
 0.978
bamE
Outer membrane protein assembly factor BamE precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
   
 
 0.956
bamB
Outer membrane protein assembly factor BamB precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
 
 0.953
rssA_2
NTE family protein RssA.
  
 
 0.898
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
 
 
   0.799
proS
Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
       0.773
lolA
Outer-membrane lipoprotein carrier protein precursor; 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).
 
   
 0.656
rlmE
Ribosomal RNA large subunit methyltransferase E; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
  
     0.639
lnt
Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation; Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily.
  
   
 0.631
tolB
Translocation 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.
  
   
 0.630
Your Current Organism:
Berkiella aquae
NCBI taxonomy Id: 295108
Other names: C. Berkiella aquae, Candidatus Berkiella aquae, Coxiellaceae bacterium HT99, Legionella-like amoebal pathogen HT99
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.