| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ctxA | ctxB | VC_1457 | VC_1456 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | 0.999 |
| ctxA | hlyA | VC_1457 | VC_A0219 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | 0.609 |
| ctxA | ompU | VC_1457 | VC_0633 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Outer membrane protein OmpU; Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.559 |
| ctxA | rtxA | VC_1457 | VC_1451 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | RTX toxin RtxA; [Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host [...] | 0.521 |
| ctxA | rtxC | VC_1457 | VC_1450 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | RTX toxin activating protein; Involved in fatty acylation of the protoxin (RtxA) at two internal lysine residues, thereby converting it to the active toxin. The acyl donor is ACP (By similarity). | 0.509 |
| ctxA | tcpA | VC_1457 | VC_0828 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Toxin co-regulated pilin; Constituent of pili, which may be involved in adhesion of V.cholerae to the host intestinal epithelium. | 0.618 |
| ctxA | toxR | VC_1457 | VC_0984 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Cholera toxin transcriptional activator; This transcription activator controls cholera toxin, pilus colonization factor and outer membrane protein expression in V.cholerae. It binds to the 5'-TTTTGAT-3' tandemly repeated DNA sequence in the cholera toxin promoter region. ToxS interacts with the C-terminal periplasmic domain of ToxR, stimulating its activity. It activates transcription at the promoters for tcpI and tcpA and this is presumably via ToxT. | 0.845 |
| ctxA | zot | VC_1457 | VC_1458 | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | Zona occludens toxin; Increases the permeability of the small intestine mucosa by affecting the structure of intercellular tight junctions (zonula occludens). | 0.812 |
| ctxB | ctxA | VC_1456 | VC_1457 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | 0.999 |
| ctxB | hlyA | VC_1456 | VC_A0219 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | 0.548 |
| ctxB | ompU | VC_1456 | VC_0633 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Outer membrane protein OmpU; Forms pores that allow passive diffusion of small molecules across the outer membrane. | 0.460 |
| ctxB | rtxA | VC_1456 | VC_1451 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | RTX toxin RtxA; [Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host [...] | 0.541 |
| ctxB | rtxC | VC_1456 | VC_1450 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | RTX toxin activating protein; Involved in fatty acylation of the protoxin (RtxA) at two internal lysine residues, thereby converting it to the active toxin. The acyl donor is ACP (By similarity). | 0.542 |
| ctxB | tcpA | VC_1456 | VC_0828 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Toxin co-regulated pilin; Constituent of pili, which may be involved in adhesion of V.cholerae to the host intestinal epithelium. | 0.618 |
| ctxB | toxR | VC_1456 | VC_0984 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Cholera toxin transcriptional activator; This transcription activator controls cholera toxin, pilus colonization factor and outer membrane protein expression in V.cholerae. It binds to the 5'-TTTTGAT-3' tandemly repeated DNA sequence in the cholera toxin promoter region. ToxS interacts with the C-terminal periplasmic domain of ToxR, stimulating its activity. It activates transcription at the promoters for tcpI and tcpA and this is presumably via ToxT. | 0.559 |
| ctxB | zot | VC_1456 | VC_1458 | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | Zona occludens toxin; Increases the permeability of the small intestine mucosa by affecting the structure of intercellular tight junctions (zonula occludens). | 0.802 |
| hlyA | ctxA | VC_A0219 | VC_1457 | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | Cholera enterotoxin, A subunit; The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring. | 0.609 |
| hlyA | ctxB | VC_A0219 | VC_1456 | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | Cholera enterotoxin, B subunit; The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. | 0.548 |
| hlyA | hlyB | VC_A0219 | VC_A0220 | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | Hemolysin secretion protein HylB; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. | 0.698 |
| hlyA | hlyU | VC_A0219 | VC_0678 | Haemolysin; Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. | Transcriptional activator HlyU; Up-regulates the expression of the hemolysin gene, hlyA, and may promote expression of other virulence determinants in vivo. It may have both positive and negative regulator activities. | 0.772 |
