ID   TACY_LISIV              Reviewed;         528 AA.
AC   P31831;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Ivanolysin;
DE   AltName: Full=Thiol-activated cytolysin;
DE   Flags: Precursor;
GN   Name=ilo;
OS   Listeria ivanovii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19119 / DSM 20750 / BCRC 14844 / JCM 7681 / KCTC 3444 / NCTC
RC   11846 / NRRL B-33017 / SLCC 2379 / WDCM 00018;
RX   PubMed=1543752; DOI=10.1016/0167-4781(92)90466-d;
RA   Haas A., Dumbsky M., Kreft J.;
RT   "Listeriolysin genes: complete sequence of ilo from Listeria ivanovii and
RT   of lso from Listeria seeligeri.";
RL   Biochim. Biophys. Acta 1130:81-84(1992).
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:P0C2E9}.
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:P13128}. Host
CC       membrane {ECO:0000250|UniProtKB:P13128}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q04IN8}. Note=Secreted as soluble protein that
CC       then inserts into the host membrane and forms pores formed by
CC       transmembrane beta-strands. {ECO:0000250|UniProtKB:Q04IN8}.
CC   -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC       {ECO:0000305}.
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DR   EMBL; X60461; CAA42995.2; -; Genomic_DNA.
DR   PIR; S22341; S22341.
DR   AlphaFoldDB; P31831; -.
DR   SMR; P31831; -.
DR   TCDB; 1.C.12.1.6; the thiol-activated cholesterol-dependent cytolysin (cdc) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell 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 membrane; Lipid-binding; Membrane; Secreted;
KW   Signal; Toxin; Transmembrane; Transmembrane beta strand; Virulence.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..528
FT                   /note="Ivanolysin"
FT                   /id="PRO_0000034100"
FT   TRANSMEM        213..226
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        233..242
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        311..320
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        328..340
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   MOTIF           482..492
FT                   /note="Conserved undecapeptide"
FT                   /evidence="ECO:0000305"
FT   MOTIF           514..515
FT                   /note="Cholesterol binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2E9"
SQ   SEQUENCE   528 AA;  58542 MW;  D133BEC1A8C51A65 CRC64;
     MKKIMLLLMT LLLVSLPLAQ EAQADASVYS YQGIISHMAP PASPPAKPKT PVEKKNAAQI
     DQYIQGLDYD KNNILVYDGE AVKNVPPKAG YKEGNQYIVV EKKKKSINQN NADIQVINSL
     ASLTYPGALV KANSELVENQ PDVLPVKRDS VTLSIDLPGM VNHDNEIVVQ NATKSNINDG
     VNTLVDRWNN KYSEEYPNIS AKIDYDQEMA YSESQLVAKF GAAFKAVNNS LNVNFGAISE
     GKVQEEVINF KQIYYTVNVN EPTSPSRFFG KSVTKENLQA LGVNAENPPA YISSVAYGRD
     IFVKLSTSSH STRVKAAFDT AFKGKSVKGD TELENIIQNA SFKAVIYGGS AKDEVEIIDG
     DLSKLRDILK QGANFDKKNP GVPIAYTTNF LKDNQLAVVK NNSEYIETTS KAYSDGKINL
     DHSGAYVARF NVTWDEVSYD ANGNEVVEHK KWSENDKDKL AHFTTSIYLP GNARNINIHA
     KECTGLAWEW WRTVVDDRNL PLVKNRNVCI WGTTLYPAYS DTVDNPIK