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
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[Homology]
Score
azo2643Putative dual specificity protein phosphatase,; Function unclear. (187 aa)    
Predicted Functional Partners:
azo1211
Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs.
   
 0.885
draG2
Putative ADP-ribosyl-[dinitrogen reductase] hydrolase. Homology to draG of R. rubrum of 24% (sprot|DRAG_RHORU) Involved in the regulation of the nitrogen fixation activity by the reversible ADP-ribosylation of the dinitrogenase reductase component of the nitrogenase enzyme complex. Pfam: ADP-ribosylglycohydrolase no signal peptide no TMHs; High confidence in function and specificity.
      0.837
azo3617
Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...]
    
 0.731
inaA
Conserved hypothetical InaA protein. Homology to inaA of P. putida of 39% (gnl|keqq|ppu:PP0904(KEGG)). Pfam: Lipopolysaccharide kinase (Kdo/WaaP) family. These lipopolysaccharide kinases are related to protein kinases Pkinase. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. e [...]
    
 0.723
waaP3
Lipopolysaccharide core biosynthesis protein. INVOLVED IN ATTACHMENT OF PHOSPHATE-CONTAINING SUBSTITUENTS TO THE INNER CORE. Specific function unclear.
    
 0.723
azo3571
Conserved hypothetical protein; InterPro: Eukaryotic protein kinase. Might be related to lipopolysaccharide biosynthesis, due to the presence of the gene in a lipopolysaccharide gene cluster.
    
 0.723
azo3573
Conserved hypothetical protein, 43% identity(65% similarity) to TrEMBL|Q9HUG7,Hypothetical protein PA4998 [PA4998] [Pseudomonas aeruginosa]. Has PF06293:IPR010440:Lipopolysaccharide kinase (Kdo/WaaP) family;These lipopolysaccharide kinases are related to protein kinases Pkinase. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it [...]
    
 0.723
lepA
Probable GTP-binding protein; 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.
   
  0.715
azo2642
Hypothetical protein, very weak homology with any hits in the database. Has, No domains, repeats, motifs or features could be predicted with confidence above threshold scores.
       0.682
pheA
Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity.
    
  0.673
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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