Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Putative inner membrane protein.

Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Putative inner membrane protein.

Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Putative inner membrane protein.

Putative autotransported protein; Pathogenicity island encoded protein: SPI3; MisL (gi|4324610).

Putative inner membrane protein.

pipB-like protein; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Involved in the reorganization of late endosome/lysosome (LE/Lys) compartments in mammalian cells. Necessary and sufficient to link kinesin-1 onto the Salmonella-containing vacuole (SCV) membrane. Required for centrifugal extension of lysosomal glycoprotein-rich membrane tubules, known as Salmonella-induced filaments (Sifs), away from the SCV and toward the cell periphery. Required for virulence, but not for intracellular survival and replication in phagocytic cells.

Putative inner membrane protein.

Cytoplasmic cell invasion protein; Required for invasion of epithelial cells; Belongs to the MxiH/PrgI/YscF family.

Putative inner membrane protein.

Lysosomal glycoprotein (lgp)-containing structures; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and formation of Salmonella-induced filaments (Sifs), which are filamentous structures containing lysosomal membrane glycoproteins within epithelial cells. Sif formation is concomitant with intracellular bacterial replication.

Putative inner membrane protein.

Salmonella translocated effector: translocated by SPI-2; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues; Belongs to the Sif family.

Putative inner membrane protein.

Cell invasion protein; Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...]

Putative inner membrane protein.

Cell invasion protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in association with its chape [...]

Putative inner membrane protein.

Cell invasion protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell.

Putative inner membrane protein.

Cell invasion protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.

Putative inner membrane protein.

Leucine-rich repeat protein; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death.

Putative inner membrane protein.

Secreted effector protein of Salmonella; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.

Putative inner membrane protein.

Pathogenicity island encoded protein: SPI5; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulti [...]

Putative inner membrane protein.

Secreted protein in the Sop family; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Contributes to replication in macrophages. Plays a role, cooperatively with SopB, in membrane fission and macropinosome formation during invasion.

Putative inner membrane protein.

Homologous to secreted protein sopD; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Contributes to the formation of Salmonella-induced filaments (Sifs) in infected epithelial cells and to replication in macrophages.

Putative inner membrane protein.

TypeIII-secreted protein effector: invasion-associated protein; Activator for CDC42 by directly engaging this Rho GTPase and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates NF-kB, p38 and ERK kinases, which are known to be involved in the induction of IL-8 expression. Chaperone InvB is required for secretion, translocation and stabilization of intracellular levels of sopE2.

Putative inner membrane protein.

Protein tyrosine phosphate; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear. In the N-terminal section; belongs to the YopE family.