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lmo0590 lmo0590 lmo1863 lmo1863 atpE atpE lmo0088 lmo0088 hly hly lmo2514 lmo2514 inlB inlB
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.
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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
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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:
lmo0590Lmo0590 protein; Similar to a fusion of two types of conserved hypothetical proteinconserved hypothetical. (588 aa)
lmo1863DegV domain-containing protein lmo1863; May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. (279 aa)
atpEATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (72 aa)
lmo0088ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (80 aa)
hlyListeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] (529 aa)
lmo2514DegV domain-containing protein lmo2514; May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. (283 aa)
inlBInternalin B; Mediates the entry of L.monocytogenes into normally non- phagocytic mammalian host cells. Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB. Downstream targets MAPK1/MAPK3 (Erk1/2) and AKT are phosphorylated in response to InlB, which also causes cell colony scattering. Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) has been suggested to also act an InlB receptor, but this is less certain. Stimulation of Tyr-phosphorylation of MET by InlB is potentiated [...] (630 aa)
Your Current Organism:
Listeria monocytogenes
NCBI taxonomy Id: 169963
Other names: L. monocytogenes EGD-e, Listeria monocytogenes ATCC BAA-679, Listeria monocytogenes EGD-e, Listeria monocytogenes EGDe, Listeria monocytogenes str. EGD-e, Listeria monocytogenes strain EGD-e
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