UniProt functional annotation for P09616



	UniProt functional annotation for P09616

UniProt code: P09616.

Organism: Staphylococcus aureus.

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Staphylococcus.

Function: Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis (PubMed:1587866, PubMed:20624979). Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866, PubMed:20624979). Heptamer oligomerization and pore formation is required for lytic activity (PubMed:1587866, PubMed:20624979). {ECO:0000269|PubMed:1587866, ECO:0000269|PubMed:20624979}.

Subunit: Self-assembles to first form a non-lytic oligomeric intermediate, and then, a mushroom-shaped homoheptamer structure of 100 Angstroms in length and up to 100 Angstroms in diameter (PubMed:8943190) (Probable). Interacts with human ADAM10; this interaction is required for toxin pore formation, disruption of focal adhesions, and hly-mediated cytotoxicity (PubMed:20624979). {ECO:0000269|PubMed:20624979, ECO:0000269|PubMed:8943190, ECO:0000305|PubMed:1400487, ECO:0000305|PubMed:1587866}.

Subcellular location: Secreted {ECO:0000269|PubMed:8943190}. Note=Secreted as a monomer (PubMed:8943190). After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand. {ECO:0000269|PubMed:8943190}.

Domain: The mushroom-shaped heptamer is composed of a cap domain (comprising 7 beta sandwiches and the amino latches of each protomer), 7 rim regions whose protruding strands may interact with the membrane bilayer, and the stem domain (52 Angstroms in length, 26 Angstroms in diameter) which forms the transmembrane pore. {ECO:0000269|PubMed:8943190}.

Similarity: Belongs to the aerolysin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Staphylococcus aureus.
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Staphylococcus.



Function:		Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis (PubMed:1587866, PubMed:20624979). Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866, PubMed:20624979). Heptamer oligomerization and pore formation is required for lytic activity (PubMed:1587866, PubMed:20624979). {ECO:0000269\|PubMed:1587866, ECO:0000269\|PubMed:20624979}.


Subunit:		Self-assembles to first form a non-lytic oligomeric intermediate, and then, a mushroom-shaped homoheptamer structure of 100 Angstroms in length and up to 100 Angstroms in diameter (PubMed:8943190) (Probable). Interacts with human ADAM10; this interaction is required for toxin pore formation, disruption of focal adhesions, and hly-mediated cytotoxicity (PubMed:20624979). {ECO:0000269\|PubMed:20624979, ECO:0000269\|PubMed:8943190, ECO:0000305\|PubMed:1400487, ECO:0000305\|PubMed:1587866}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:8943190}. Note=Secreted as a monomer (PubMed:8943190). After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand. {ECO:0000269\|PubMed:8943190}.
Domain:		The mushroom-shaped heptamer is composed of a cap domain (comprising 7 beta sandwiches and the amino latches of each protomer), 7 rim regions whose protruding strands may interact with the membrane bilayer, and the stem domain (52 Angstroms in length, 26 Angstroms in diameter) which forms the transmembrane pore. {ECO:0000269\|PubMed:8943190}.
Similarity:		Belongs to the aerolysin family. {ECO:0000305}.