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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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
tolATolA, involved in the tonB-independent uptake of proteins, interacts with the TolQ and TolR, cytoplasmic membrane proteins and with the Pal protein (OprL) in the outer membrane. The transport is energized by the proton motive force. The Tol-Pal complex is required for maintaining outer membrane integrity, the transport (uptake) filamentous DNA and is the conduct for bacteriophages; TolA is anchored to the cytoplasmic membrane by a single transmembrane spanning segment near the N-terminus, leaving most of the protein exposed to the periplasm; High confidence in function and specificity. (313 aa)    
Predicted Functional Partners:
tolR
TolR, involved in the tonB-independent uptake of biopolymers, forms a complex with the proteins TolQ. This complex energizes TolA from the potential energy of the ion electrochemical gradient. TolA energized, interacts with the outer membrane protein Pal (OprL). The Tol-Pal complex is required for maintaining outer membrane integrity, the transport (uptake) filamentous DNA and is the conduct for bacteriophages; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
 
 
 0.957
tolQ
TolQ, involved in the tonB-independent uptake of biopolymers, forms a complex with the proteins TolR. This complex energizes TolA from the potential energy of the ion electrochemical gradient. TolA energized, interacts with the outer membrane protein Pal (OprL). The Tol-Pal complex is required for maintaining outer membrane integrity, the transport (uptake) filamentous DNA and is the conduct for bacteriophages; Contains three transmembrane helices; Belongs to the exbB/tolQ family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
 
 
 0.945
CAZ96885.1
Possible 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; The signal peptide is cleaved between the residues 21 and 22; Family membership.
 
 
 0.850
CAZ97258.1
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 (34-108) and the Plug module (124-231) acting as a channel gate; The signal peptide is cleaved between the residues 30 and 31; Family membership.
  
 
 0.848
CAZ94114.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein.
 
 
 0.817
CAZ96884.1
TPR repeat-containing protein; Protein that contains at least ten Tetratricopeptide repeat (TPR) domains involved in the proteinprotein interactions and the assembly of multiprotein complexes; Signal peptide cleavbed between the residues 21 and 22; Localized in the periplasmic space; Function unclear.
 
   
 0.770
folC
Bifunctional enzyme that converts the folates to polyglutamate derivatives; Folylpolyglutamate synthase (EC 6.3.2.17) is responsible for the ATP-dependent addition of a polyglutamate tail to tetrahydrofolate. Dihydrofolate synthase (EC 6.3.2.12) is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate. The combined activity leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlu(n)), i.e. various tetrahydrofolates (H4folate); Localized in the cytoplasm; High confidence in function and specificity.
       0.768
exbD1
ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
 
 
 0.763
CAZ95254.1
TPR repeats protein; Conserved protein containing three tetratrico peptide repeats (TPRs). TPR repeats mediate proteinprotein interactions and the assembly of multiprotein complexes; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Family membership.
  
     0.760
CAZ98193.1
Conserved hypothetical membrane protein; Contains an uncleavable signal sequence; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
     0.717
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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