ID   TACY_BACCE              Reviewed;         485 AA.
AC   Q45105;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Hemolysin;
DE   Flags: Precursor; Fragment;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RIMD 206001;
RX   PubMed=8063419; DOI=10.1128/iai.62.9.4000-4004.1994;
RA   Yutsudo T., Okumura K., Iwasaki M., Hara A., Kamitani S., Minamide W.,
RA   Igarashi H., Hinuma Y.;
RT   "The gene encoding a new mitogenic factor in a Streptococcus pyogenes
RT   strain is distributed only in group A streptococci.";
RL   Infect. Immun. 62:4000-4004(1994).
CC   -!- FUNCTION: A cholesterol-dependent toxin with hemolytic activity against
CC       host red blood cells. Causes cytolysis by forming pores in cholesterol
CC       containing host membranes. binding to target membranes, the protein
CC       undergoes a major conformation change, leading to its insertion in the
CC       host membrane and formation of an oligomeric pore complex. Cholesterol
CC       is required for binding to host membranes, membrane insertion and pore
CC       formation; cholesterol binding is mediated by a Thr-Leu pair in the C-
CC       terminus. Can be reversibly inactivated by oxidation.
CC       {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:P13128}. Host
CC       cell membrane {ECO:0000250|UniProtKB:P13128}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q04IN8}. Note=Secreted as soluble
CC       protein that then inserts into the host cell membrane and forms pores
CC       formed by 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; D21270; BAA04808.1; -; Genomic_DNA.
DR   PIR; I39863; I39863.
DR   AlphaFoldDB; Q45105; -.
DR   SMR; Q45105; -.
DR   STRING; 1396.DJ87_1640; -.
DR   eggNOG; ENOG502Z7ST; Bacteria.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..>485
FT                   /note="Hemolysin"
FT                   /id="PRO_0000034111"
FT   TRANSMEM        196..209
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        216..225
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        294..303
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   TRANSMEM        311..323
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT   MOTIF           465..475
FT                   /note="Conserved undecapeptide"
FT                   /evidence="ECO:0000305"
FT   NON_TER         485
SQ   SEQUENCE   485 AA;  53863 MW;  9956BC17769396D2 CRC64;
     MKNFKGRKFL TCVLVSLCTL NYSSISFAET QAGHANDITK NASSIDTGIG NLTYNNQEVL
     AVNGDKVESF VPKESINSNG KFVVVDVRKN HLQRHQSIFR LLDSVANRTY PGAVQLANKA
     FADNQPSLLV AKRKPLNISI DLPGMRKENT ITVQNPTYGN VAGAVDDLVS TWNEKYSATH
     TLPARMQYTE SMVYSKAQIA SALNVNAKYL DNSLNIDFNA VANGEKKVMV AAYKQIFYTV
     SAELPNNPSD LFDNSVTFGE LTRKGVSNSA PPVMVSNVAY GRTVYVKLET TSKSKDVQAA
     FKALLKNNSV ETSGQYKDIF EESTFTAVVL GGDAKEHNKV VTKDFNEIRN IIKDNAELSF
     KNPAYPISYT STFLKDNATA AVHNNTDYIE TTTTEYSSAK MTLDHYGAYV AQFDVSWDGF
     TFDQNGKEIL THKTWEGSGK DKTAHYSTVI PLPPNSKNIK IVARECTGLA WEWWRTIIKM
     NKMFH