UniProt functional annotation for P18013



	UniProt functional annotation for P18013

UniProt code: P18013.

Organism: Shigella flexneri.

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella.

Function: Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal. {ECO:0000269|PubMed:15731041, ECO:0000269|PubMed:7957095}.

Subcellular location: Secreted {ECO:0000269|PubMed:17077085}. Note=Secreted via the type III secretion system (TTSS). Localizes to the tip of the external secretion needle that is part of the TTSS apparatus.

Induction: Synthesis of this immunogen is repressed at 30 degrees Celsius and restored at 37 degrees Celsius.

Domain: The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors.

Miscellaneous: Deletion of amino acids 1-20 abolishes invasion activity, affects contact-mediated hemolysis activity and IpaD secretion. Deletion of amino acids 41-80 and 81-120 restores invasion activity to a higher level than wild-type and reduces contact-mediated hemolysis activity. Deletion beyond amino acid 120 reduces invasion activity and abolishes contact-mediated hemolysis activity.

Similarity: Belongs to the invasin protein D family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Shigella flexneri.
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella.



Function:		Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal. {ECO:0000269\|PubMed:15731041, ECO:0000269\|PubMed:7957095}.


Subcellular location:		Secreted {ECO:0000269\|PubMed:17077085}. Note=Secreted via the type III secretion system (TTSS). Localizes to the tip of the external secretion needle that is part of the TTSS apparatus.
Induction:		Synthesis of this immunogen is repressed at 30 degrees Celsius and restored at 37 degrees Celsius.
Domain:		The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors.
Miscellaneous:		Deletion of amino acids 1-20 abolishes invasion activity, affects contact-mediated hemolysis activity and IpaD secretion. Deletion of amino acids 41-80 and 81-120 restores invasion activity to a higher level than wild-type and reduces contact-mediated hemolysis activity. Deletion beyond amino acid 120 reduces invasion activity and abolishes contact-mediated hemolysis activity.
Similarity:		Belongs to the invasin protein D family. {ECO:0000305}.