TACY_STRPQ
ID TACY_STRPQ Reviewed; 571 AA.
AC P0DF97; P0A4L0; P21131;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Streptolysin O;
DE Short=SLO;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=slo; OrderedLocusNames=SPs0132;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
RN [2]
RP FUNCTION, CHOLESTEROL-BINDING, AND MUTAGENESIS OF 561-THR-LEU-562.
RX PubMed=20145114; DOI=10.1073/pnas.0911581107;
RA Farrand A.J., LaChapelle S., Hotze E.M., Johnson A.E., Tweten R.K.;
RT "Only two amino acids are essential for cytolytic toxin recognition of
RT cholesterol at the membrane surface.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4341-4346(2010).
RN [3] {ECO:0007744|PDB:4HSC}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND DOMAIN.
RC STRAIN=SSI-1;
RX PubMed=24316049; DOI=10.1016/j.jmb.2013.11.020;
RA Feil S.C., Ascher D.B., Kuiper M.J., Tweten R.K., Parker M.W.;
RT "Structural studies of Streptococcus pyogenes streptolysin O provide
RT insights into the early steps of membrane penetration.";
RL J. Mol. Biol. 426:785-792(2014).
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:0000269|PubMed:20145114}.
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}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04IN8}. Note=Probably secreted as soluble
CC protein by the accessory Sec system (By similarity). It then inserts
CC into the host cell membrane and forms pores formed by transmembrane
CC beta-strands (By similarity). {ECO:0000250|UniProtKB:P0C2J9,
CC ECO:0000250|UniProtKB:Q04IN8}.
CC -!- DOMAIN: Mature protein (about residues 103 to 571) has 3 discontinuous
CC domains; D1 (residues 103-124, 161-249, 300-345 and 421-444), D2
CC (residues 125-160 and 445-461), D3 (residues 250-299 and 346-420)
CC followed by C-terminal D4 (residues 462-571).
CC {ECO:0000269|PubMed:24316049}.
CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC63227.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000034; BAC63227.1; ALT_INIT; Genomic_DNA.
DR PIR; A43507; A43507.
DR RefSeq; WP_010921831.1; NC_004606.1.
DR PDB; 4HSC; X-ray; 2.10 A; X=1-571.
DR PDBsum; 4HSC; -.
DR AlphaFoldDB; P0DF97; -.
DR SMR; P0DF97; -.
DR GeneID; 57851997; -.
DR KEGG; sps:SPs0132; -.
DR HOGENOM; CLU_026912_1_0_9; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Hemolysis; Host cell membrane; Host membrane;
KW Lipid-binding; 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_0000411588"
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 30..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 564..565
FT /note="Cholesterol binding"
FT /evidence="ECO:0000269|PubMed:20145114"
FT COMPBIAS 30..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"
FT MUTAGEN 561..562
FT /note="TL->GG: Loss of hemolytic activity, loss of host
FT membrane binding, loss of cholesterol binding."
FT /evidence="ECO:0000269|PubMed:20145114"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 143..158
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 291..306
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 336..354
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:4HSC"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 429..437
FT /evidence="ECO:0007829|PDB:4HSC"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 448..461
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 472..486
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:4HSC"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 506..516
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 537..547
FT /evidence="ECO:0007829|PDB:4HSC"
FT STRAND 551..571
FT /evidence="ECO:0007829|PDB:4HSC"
SQ SEQUENCE 571 AA; 63638 MW; D05AA9979DCBCAB0 CRC64;
MSNKKTFKKY SRVAGLLTAA LIIGNLVTAN AESNKQNTAS TETTTTNEQP KPESSELTTE
KAGQKTDDML 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 TFKELQRKGV 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
