TACY_STRP6
ID TACY_STRP6 Reviewed; 571 AA.
AC Q5XE40;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Streptolysin O;
DE Short=SLO;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=slo; OrderedLocusNames=M6_Spy0188;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT86323.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000003; AAT86323.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5XE40; -.
DR SMR; Q5XE40; -.
DR EnsemblBacteria; AAT86323; AAT86323; M6_Spy0188.
DR KEGG; spa:M6_Spy0188; -.
DR HOGENOM; CLU_026912_1_0_9; -.
DR Proteomes; UP000001167; Chromosome.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..571
FT /note="Streptolysin O"
FT /id="PRO_0000034109"
FT TRANSMEM 260..273
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 280..289
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 358..367
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 375..387
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT REGION 32..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 529..539
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 561
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
FT COMPBIAS 32..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 63695 MW; 95B1DBEAEB50CAB0 CRC64;
MSNKKTFKKY SRVAGLLTVA LIIGNLVTAN AESNKQNTAS TETTTTNEQP KPESSELTIE
KAGQKMDDML NSNDMIKLAP KEMPLESAEK EEKKSEDKKK SEEDHTEEIN DKIYSLNYNE
LEVLAKNGET IENFVPKEGV KKADKFIVIE RKKKNINTTP VDISIIDSVT DRTYPAALQL
ANKGFTENKP DAVVTKRNPQ KIHIDLPGMG DKATVEVNDP TYANVSTAID NLVNQWHDNY
SGGNTLPART QYTESMVYSK SQIEAALNVN SKILDGTLGI DFKSISKGEK KVMIAAYKQI
FYTVSANLPN NPADVFDKSV TFKDLQRKGV SNEAPPLFVS NVAYGRTVFV KLETSSKSND
VEAAFSAALK GTDVKTNGKY SDILENSSFT AVVLGGDAAE HNKVVTKDFD VIRNVIKDNA
TFSRKNPAYP ISYTSVFLKN NKIAGVNNRT EYVETTSTEY TSGKINLSHQ GAYVAQYEIL
WDEINYDDKG KEVITKRRWD NNWYSKTSPF STVIPLGANS RNIRIMAREC TGLAWEWWRK
VIDERDVKLS KEINVNISGS TLSPYGSITY K
