ID   OLYA6_PLEOS             Reviewed;         138 AA.
AC   P83467; M4QNV2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Ostreolysin A6;
GN   Name=OlyA6;
OS   Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=5322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=23806422; DOI=10.1016/j.biochi.2013.06.012;
RA   Ota K., Leonardi A., Mikelj M., Skocaj M., Wohlschlager T., Kunzler M.,
RA   Aebi M., Narat M., Krizaj I., Anderluh G., Sepcic K., Macek P.;
RT   "Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory
RT   for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin
RT   B.";
RL   Biochimie 95:1855-1864(2013).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-51, FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Plo 5; TISSUE=Fruiting body;
RX   PubMed=12020804; DOI=10.1016/s0304-4165(02)00190-3;
RA   Berne S., Krizaj I., Pohleven F., Turk T., Macek P., Sepcic K.;
RT   "Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in
RT   fungal fruiting.";
RL   Biochim. Biophys. Acta 1570:153-159(2002).
CC   -!- FUNCTION: Has hemolytic activity against bovine erythrocytes at
CC       nanomolar concentrations in vitro. Promotes active pleurotolysin B
CC       (PlyB)-dependent permeabilization of membranes rich in cholesterol and
CC       sphingomyelin. May play an important role in the initial phase of
CC       fungal fruiting. {ECO:0000269|PubMed:12020804,
CC       ECO:0000269|PubMed:23806422}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12020804}.
CC   -!- DEVELOPMENTAL STAGE: Expression begins during formation of the
CC       primordia, increases remarkably as the fruiting bodies develop and
CC       declines as they mature. {ECO:0000269|PubMed:12020804}.
CC   -!- SIMILARITY: Belongs to the aegerolysin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KC012711; AGH25589.1; -; mRNA.
DR   PDB; 6MYI; X-ray; 1.15 A; A/B/C/D=1-138.
DR   PDB; 6MYJ; X-ray; 1.33 A; A/B/C/D=1-138.
DR   PDB; 6MYK; X-ray; 1.80 A; A/B/C/D=1-138.
DR   PDBsum; 6MYI; -.
DR   PDBsum; 6MYJ; -.
DR   PDBsum; 6MYK; -.
DR   AlphaFoldDB; P83467; -.
DR   SMR; P83467; -.
DR   TCDB; 1.C.119.1.2; the aegerolysin (aegerolysin) family.
DR   TCDB; 1.C.97.3.2; the pleurotolysin pore-forming (pleurotolysin) family.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1090164; -.
DR   GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR009413; Aegerolysin-typ.
DR   Pfam; PF06355; Aegerolysin; 1.
DR   PIRSF; PIRSF007951; PIRSF007951; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Hemolysis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12020804"
FT   CHAIN           2..138
FT                   /note="Ostreolysin A6"
FT                   /id="PRO_0000156988"
FT   STRAND          6..13
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          19..33
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   TURN            80..84
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:6MYI"
FT   STRAND          127..135
FT                   /evidence="ECO:0007829|PDB:6MYI"
SQ   SEQUENCE   138 AA;  15093 MW;  F2A51BD2DC21426A CRC64;
     MAYAQWVIII IHNVGSQDVK IKNLKASWGK LHADGDKDAE VSASNYEGKI VKPDEKLQIN
     ACGRSDAAEG TTGTFDLVDP ADGDKQVRHF YWDCPWGSKT NTWTVSGSNT KWMIEYSGQN
     LDSGALGTIT VDTLKKGN