ID   TACY_STRCB              Reviewed;         574 AA.
AC   Q53957;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Streptolysin O;
DE            Short=SLO;
DE   AltName: Full=Thiol-activated cytolysin;
DE   Flags: Precursor;
GN   Name=slo;
OS   Streptococcus canis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7803818; DOI=10.3109/10425179409020859;
RA   Okumura K., Hara A., Tanaka T., Nichiguchi I., Minamide W., Igarashi H.,
RA   Yutsudo T.;
RT   "Cloning and sequencing the streptolysin O genes of group C and group G
RT   streptococci.";
RL   DNA Seq. 4:325-328(1994).
CC   -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by
CC       forming pores in cholesterol containing host membranes. After binding
CC       to target membranes, the protein undergoes a major conformation change,
CC       leading to its insertion in the host membrane and formation of an
CC       oligomeric pore complex. Cholesterol is required for binding to host
CC       membranes, membrane insertion and pore formation; cholesterol binding
CC       is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly
CC       inactivated by oxidation. {ECO:0000250|UniProtKB:P13128}.
CC   -!- SUBUNIT: Homooligomeric pore complex of 35 to 50 subunits; when
CC       inserted in the host membrane. {ECO:0000250|UniProtKB:Q04IN8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C2J9}. Host
CC       cell membrane {ECO:0000250|UniProtKB:P13128}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q04IN8}. Note=Probably secreted as
CC       soluble protein by the accessory Sec system (By similarity). It then
CC       inserts into the host cell membrane and forms pores formed by
CC       transmembrane beta-strands (By similarity).
CC       {ECO:0000250|UniProtKB:P0C2J9, ECO:0000250|UniProtKB:Q04IN8}.
CC   -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC       {ECO:0000305}.
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DR   EMBL; D16825; BAA04105.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53957; -.
DR   SMR; Q53957; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015485; F:cholesterol binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1430; -; 1.
DR   Gene3D; 3.90.840.10; -; 1.
DR   InterPro; IPR035390; Thiol_cytolys_C.
DR   InterPro; IPR038700; Thiol_cytolys_C_sf.
DR   InterPro; IPR001869; Thiol_cytolysin.
DR   InterPro; IPR036363; Thiol_cytolysin_ab_sf.
DR   InterPro; IPR036359; Thiol_cytolysin_sf.
DR   Pfam; PF17440; Thiol_cytolys_C; 1.
DR   Pfam; PF01289; Thiol_cytolysin; 1.
DR   PRINTS; PR01400; TACYTOLYSIN.
DR   SUPFAM; SSF56978; SSF56978; 1.
DR   PROSITE; PS00481; THIOL_CYTOLYSINS; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Hemolysis; Host cell membrane; Host membrane; Lipid-binding;
KW   Membrane; Secreted; Signal; Toxin; Transmembrane;
KW   Transmembrane beta strand; Virulence.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..574
FT                   /note="Streptolysin O"
FT                   /id="PRO_0000034105"
FT   TRANSMEM        263..276
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        283..292
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        361..370
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        378..390
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   REGION          37..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           532..542
FT                   /note="Conserved undecapeptide"
FT                   /evidence="ECO:0000305"
FT   MOTIF           564..565
FT                   /note="Cholesterol binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2E9"
FT   COMPBIAS        37..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  63911 MW;  C84D2036908329AF CRC64;
     MKDMSNKKIF KKYSRVAGLL TAALIVGNLV TANADSNKQN TANTETTTTN EQPKPESSEL
     TTEKAGQKMD DMLNSNDMIK LAPKEMPLES AEKEEKKSED NKKSEEDHTE EINDKIYSLN
     YNELEVLAKN GETIENFVPK EGVKKADKFI VIERKKKNIN TTPVDISIID SVTDRTYPAA
     LQLANKGFTE NKPDAVVTKR NPQKIHIDLP GMGDKATVEV NDPTYANVST AIDNLVNQWH
     DNYSGGNTLP ARTQYTESMV YSKSQIEAAL NVNSKILDGT LGIDFKSISK GEKKVMIAAY
     KQIFYTVSAN LPNNPADVFD KSVTFKELQA KGVSNEAPPL FVSNVAYGRT VFVKLETSSK
     SNDVEAAFSA ALKGTDVKTN GKYSDILENS SFTAVVLGAD AAEHNKVVTK DFDVIRNVIK
     ANATFSRKNP AYPISYTSVF LKNNKIAGVN NRSEYVETTS TEYTSGKINL SHQGAYVAQY
     EILWDEINYD DKGKEVITKR RWDNNWYSKT SPFSTVIPLG ANSRNIRIMA RECTGLAWEW
     WRKVIDERDV KLSKEINVNI SGSTLSPYGS ITYK