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
CAZ94641.1TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (57-134) and the Plug module (152-258) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. (823 aa)    
Predicted Functional Partners:
CAZ94642.1
Putative membrane lipoprotein; Contains a lipoprotein signal peptide cleaved between the residues 17 and 18; Probably localized in the outer membrane; Hypothetical protein.
       0.773
CAZ98031.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules (here possibly sugars) that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (26-98) and the Plug module (114-224) acting as a channel gate; The signal peptide is cleaved between the residues 24 and 25; Family membership.
  
    0.641
CAZ96822.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules (here, possibly sugars) that are too large to diffuse via the outer membrane porins or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-96), the Plug module (112-227) acting as the channel gate and a pectinesterase signature (404-423); The signal peptide is cleaved between the residue 25 and 26; Family membership.
  
    0.628
CAZ96162.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (33-106) and the Plug module (122-228) acting as a channel gate; The signal peptide is cleaved between the residues 31 and 32; Family membership.
  
    0.623
CAZ98834.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (34-107) and the Plug module (123-228) acting as a channel gate; The signal peptide is cleaved between the residues 27 and 28; Family membership.
  
    0.620
CAZ94314.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (43-117) and the Plug module (133-240) acting as a channel gate; The signal peptide is cleaved between the residues 25 and 26; Family membership.
  
    0.612
tonB1
TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family.
 
 
 0.609
CAZ95114.1
TonB-dependent Transducer; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins; The presence of an additional N-terminal extension (Secretin/TonB (STN) domain (49-100)) that probably interacts with an anti-sigma factor, would be responsible of the signal transduction; Contains a carboxypeptidase regulatory domain (122-196), and a Plug module (212-338) acting as the channel gate; The signal peptide is cleaved between the residue 22 and 23; Family membership.
  
    0.585
CAZ94426.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (24-97) and the Plug module (113-222) acting as a channel gate; The signal peptide is cleaved between the residues 21 and 22; Family membership.
  
     0.574
tonB2
TonB protein; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Belongs to the TonB family.
 
 
 0.563
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.