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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
msbA_1Lipid A export permease/ATP-binding protein MsbA; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. (584 aa)    
Predicted Functional Partners:
gsiA_7
Oligopeptide ABC transporter ATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ABC transporter superfamily.
     
0.830
lepA
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
 
  
 0.806
atpD
F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
    
 
 0.726
recA
Recombinase RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
   
 
 0.711
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.
      
 0.682
lpxC
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the LpxC family.
 
   
 0.674
kdsD
Arabinose-5-phosphate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SIS family. GutQ/KpsF subfamily.
 
   
 0.664
lgrD_1
Peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.664
dnaK_2
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.661
lpxB
lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
   
 0.642
Your Current Organism:
Pandoraea pulmonicola
NCBI taxonomy Id: 93221
Other names: ATCC BAA-62, ATCC:BAA:62, CCUG 38759, CIP 106625, DSM 16583, LMG 18106, LMG:18106, NCTC 13159, P. pulmonicola, Pandoraea pulmonicola Coenye et al. 2000
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