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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
azo3770Conserved hypothetical protein, 43% identity (60% similarity) to TrEMBL; Q8ZML9. TrEMBL;Q8X937(44% identity to Escherichia coli) Has PF04972, Putative phospholipid-binding domain;IPR007055, TAD; This domain is found in a family of osmotic shock protection proteins (e.g. P27291). It is also found in some Secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. Has SMART;SM00257,LysM, Lysin motif:IPR002482; This domain is about 40 residues long and is found in a variety of enzymes involved in bacterial cell wall degradation. This domain [...] (164 aa)    
Predicted Functional Partners:
pilQ
Type 4 fimbrial biogenesis protein PilQ, similarity to sprot|PILQ_PSEAE (41%) and trembl|Q8XV60 (45%). PilQ is essential for the biogenesis of type IV pili. Its precise function is unknown, but it has been suggested that it may act as a pilus channel in the final stages of pilus assembly. InterPro (PF00263): General (type II) secretion pathway (GSP) D protein SignalP reporting signal peptide; Specificity unclear.
 
 
 
 0.853
gspD2
Protein D is involved in the type II general secretion pathway within Gram-negative bacteria, a signal sequence-dependent process responsible for protein export. The most probable location of protein D is the outer membrane. This suggests that protein D constitutes the apparatus of the accessory mechanism, and is thus involved in transporting exoproteins from the periplasm, across the outer membrane, to the extracellular environment. Similar to trembl|Q8XTG8 (39%). Pfam (PF00263): General (type II) secretion pathway (GSP) D protein Pfam (PF07660): Secretin and TonB N terminus short dom [...]
   
 
 0.834
azo3667
Conserved hypothetical membrane protein. Homology to RS05100 of Ralstonia solanacearum of 50% (trembl|Q8Y1D7(SRS)). Has PF05957, Bacterial protein of unknown function (DUF883);IPR010279; This family consists of several hypothetical bacterial proteins of unknown function. no signal peptide. 1 TMH; Conserved hypothetical protein.
   
  
 0.718
azo0483
Conserved hypothetical secreted protein. Homology to PA4874 of P.aeruginosa of 36% (trembl|Q9HUT9(SRS)) No domains predicted. Signal petide present. No TMH present; Conserved hypothetical protein.
  
    0.712
azo1752
Conserved hypothetical secreted protein: Homology to ne0129 of N. europaea of 43% (trembl|Q82XW6). Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. signal peptide. no TMHs; Conserved hypothetical protein.
  
  
 0.695
azo1764
Conserved hypothetical secreted protein. Homology to bb3588 of B. bronchiseptica of 41% (trembl|Q7WGK1). Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. signal peptide. TMH in signal peptide; Conserved hypoth [...]
  
  
 0.695
pilP
Type 4 fimbrial biogenesis protein, PilP. PilP is essential for the biogenesis of type IV pili. Similar to trembl|Q7NZU1(37%). SignalP reporting Signal Peptide; Family membership.
    
   0.670
pilO
Type 4 fimbrial biogenesis protein PilO, similarity to pir|S77728 (40%). PilO proteins are involved in the assembly of pilin. TMHMM reporting one TMH; Specificity unclear.
    
   0.670
pilN
Type 4 fimbrial biogenesis protein PilN, similarity to trembl|Q82SK2(51%)and to pir|S77727(42%). In P. aeruginosa PilN was found to be required for fimbrial biogenesis by complementation studies using twitching motility and sensitivity to fimbrial-specific phage as indicators of the presence of functional fimbriae. SignalP reporting signal peptide; Specificity unclear.
    
   0.670
pilM
Type 4 fimbrial biogenesis protein PilM, similarity to trembl|Q82SK1 (56%)and to pir|S77726 (47%). Four genes,pilM-P, encode the necessary proteins and pilM is required for the assembly of the type IV fimbriae in Pseudomonas aeruginosa; Specificity unclear.
    
   0.670
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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