Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Internalin 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 [...]

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Internalin J; Involved in several steps of L.monocytogenes infection by both intravenous and oral infection. Probably acts as an adhesion; upon ectopic expression in L.innocula bacteria adhere better to human cell lines.

Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for induced thermotolerance, bu [...]

Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]

Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for induced thermotolerance, bu [...]

Excinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.

Endopeptidase Clp ATP-binding chain C; Belongs to the ClpA/ClpB family.

Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]

Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]

Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for induced thermotolerance, bu [...]

Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]

Endopeptidase Clp ATP-binding chain C; Belongs to the ClpA/ClpB family.

Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]

Excinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.

Glucosamine-1-phosphate N-acetyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Internalin 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 [...]

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Internalin J; Involved in several steps of L.monocytogenes infection by both intravenous and oral infection. Probably acts as an adhesion; upon ectopic expression in L.innocula bacteria adhere better to human cell lines.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

P60 extracellular protein, invasion associated protein Iap; This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria; Belongs to the peptidase C40 family.

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Internalin 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 [...]

Internalin A; Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin- 2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA ; Belongs to the internalin family.

Internalin J; Involved in several steps of L.monocytogenes infection by both intravenous and oral infection. Probably acts as an adhesion; upon ectopic expression in L.innocula bacteria adhere better to human cell lines.

Internalin 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 [...]

Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.