Acetylornithine transaminase; Involved in both the arginine and lysine biosynthetic pathways.

Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.

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; 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.

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.

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.

Putative inner membrane protein.

Secretion system effector; SseF (gi|3377868).

Putative inner membrane protein.

Secretion system effector; SseG (gi|3377858).

Putative inner membrane protein.

Salmonella translocated effector; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and negatively regulates the formation of Salmonella-induced filaments (Sifs) in epithelial cells. Has both deacylase and esterification activities in vitro, but esterification is probably the dominant activity in host cells. Significantly contributes to cholesterol esterification, which reduces cellular cholesterol in cells and abrogates the ability of SifA to associate with cholesterol and LAMP-1 v [...]

Sensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.

Acetylornithine transaminase; Involved in both the arginine and lysine biosynthetic pathways.

Putative disulfide oxidoreductase; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein (By similarity); Belongs to the DsbB family.

Putative disulfide isomerase; Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.

Putative disulfide oxidoreductase; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein (By similarity); Belongs to the DsbB family.

Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family.

Putative disulfide isomerase; Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.

Putative disulfide oxidoreductase; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein (By similarity); Belongs to the DsbB family.

Putative disulfide isomerase; Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.

Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family.

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; 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; [...]

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 [...]

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; [...]

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.

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; [...]

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.