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
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Textmining
[Homology]
Score
CAZ97019.1TonB-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 (23-96) and the Plug module (114-236) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. (982 aa)    
Predicted Functional Partners:
CAZ97018.1
Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21, Localized in the outer membrane; Hypothetical protein.
       0.659
hisC2
The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity.
 
     0.629
CAZ96243.1
SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Contains a lipoprotein signal peptide cleaved between the residues 16 and 17; Putatively localized in the outer membrane but the determination of the membrane identity for the protein localization is not clear; it is possible that this protein be localized in both membranes; Family membership.
  
 
   0.547
CAZ97016.1
Hypothetical membrane protein; Possible permease that consists to eleven transmembrane segments; Localized in the cytoplasmic membrane; Hypothetical protein.
 
     0.509
CAZ95996.1
SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 27 and 28; Probably localized in the outer membrane; Family membership.
  
 
   0.479
dppA1
Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...]
  
     0.469
dppA2
Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 21 and 22. Localiz [...]
  
     0.423
CAZ97081.1
Conserved hypothetical lipoprotein; Protein containing a bacterial Ig-like domain 1 (Big-1). Big-1 domains (~95 amino acids) are usually present in bacterial adhesion molecules of the intimin/invasin family, involved in pathogenicity. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 25 and 26; Localized in the outer membrane; Conserved hypothetical protein.
  
 
   0.412
CAZ95738.1
Conserved hypothetical membrane protein; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
     0.401
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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