UniProt functional annotation for P09167



	UniProt functional annotation for P09167

UniProt code: P09167.

Organism: Aeromonas hydrophila.

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.

Function: Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. {ECO:0000269|PubMed:10428840, ECO:0000269|PubMed:16424900, ECO:0000269|PubMed:21779171, ECO:0000269|PubMed:23912165, ECO:0000269|PubMed:9442081}.

Subunit: Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane. {ECO:0000269|PubMed:10428840, ECO:0000269|PubMed:16424900, ECO:0000269|PubMed:23912165, ECO:0000269|PubMed:9442081}.

Subcellular location: Secreted. Host cell membrane. Note=Secreted as a soluble precursor.

Domain: The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. {ECO:0000269|PubMed:21779171}.

Ptm: Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane.

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

Sequence caution: Sequence=AAA21938.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Aeromonas hydrophila.
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.



Function:		Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. {ECO:0000269\|PubMed:10428840, ECO:0000269\|PubMed:16424900, ECO:0000269\|PubMed:21779171, ECO:0000269\|PubMed:23912165, ECO:0000269\|PubMed:9442081}.


Subunit:		Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane. {ECO:0000269\|PubMed:10428840, ECO:0000269\|PubMed:16424900, ECO:0000269\|PubMed:23912165, ECO:0000269\|PubMed:9442081}.
Subcellular location:		Secreted. Host cell membrane. Note=Secreted as a soluble precursor.
Domain:		The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. {ECO:0000269\|PubMed:21779171}.
Ptm:		Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane.
Similarity:		Belongs to the aerolysin family. {ECO:0000305}.
Sequence caution:		Sequence=AAA21938.1; Type=Frameshift; Evidence={ECO:0000305};