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
azo1765Conserved hypothetical membrane protein. Homology to Atu4467 of Agrobacterium tumefaciens of 58% (trembl|Q8U7I2). Has PF07043, Protein of unknown function (DUF1328);IPR009760;This family consists of several hypothetical bacterial proteins of around 50 residues in length. The function of this family is unknown. signal peptide. 1 TMHs; Conserved hypothetical protein. (57 aa)    
Predicted Functional Partners:
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 [...]
  
    0.814
azo1750
Hypothetical membrane protein. No homology of the entire protein to the data bank. Has DUF1328(Protein of Unknown family) domain. PF07043;IPR009760; This family consists of several hypothetical bacterial proteins of around 50 residues in length. The function of this family is unknown. no signal peptide. 3 TMHs.
  
     0.699
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.
  
    0.676
bfr3
Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity.
  
    0.664
azo0869
Conserved hypothetical secreted protein. Homology to rsc3264 of R. solanacearum (trembl|Q8XUC7). 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; outside of this group the distribution is more disparate. signal [...]
  
    0.529
azo1747
Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions.
  
    0.507
azo1751
Conserved hypothetical secreted protein. Homology to ebA6968 of Azoarcus sp. EbN1 of 38% (gnl|keqq|eba:ebA6968(KEGG)). Pfam: Putative phospholipid-binding domain 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. No TMHs. Signal peptide present; Conserved hypothetical protein.
  
    0.507
azo1819
Hypothetical protein. Homology to dr0392 of D. radiodurans of 25% (trembl|Q9RXC3) 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. no signal peptide no TMHs; High confidence in function and specificity.
  
    0.507
azo2561
Conserved hypothetical protein. Homology to dr0392 of D. radiodurans of 33% (trembl|Q9RXC3). Pfam: Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. 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 [...]
  
    0.507
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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