close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
lptDHypothetical protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (868 aa)    
Predicted Functional Partners:
surA
Molecular chaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
 
  
 0.932
lptE
Hypothetical protein; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
 
 
 
 0.913
pdxA
4-hydroxythreonine-4-phosphate dehydrogenase PdxA; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
  
    0.840
bamA
Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
  
  
 0.808
lptA
Lipopolysaccharide transport periplasmic protein LptA; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.
 
 
 0.798
AQQ66571.1
Phosphotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.763
rsmA
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))- dimethyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
  
  
 0.757
bamD
Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
  
 0.749
AQQ68402.1
LPS export ABC transporter permease LptF; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.742
AQQ66566.1
Bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family.
 
    0.726
Your Current Organism:
Microbulbifer agarilyticus
NCBI taxonomy Id: 260552
Other names: DSM 19200, JCM 14708, M. agarilyticus, Microbulbifer agarilyticus Miyazaki et al. 2008, Microbulbifer sp. JAMB-A3, Microbulbifer sp. JAMM 0654, Microbulbifer sp. JAMM 0793, strain JAMB A3
Server load: low (26%) [HD]