TACY_PAEAL
ID TACY_PAEAL Reviewed; 501 AA.
AC P23564;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Alveolysin;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=alv;
OS Paenibacillus alvei (Bacillus alvei).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44250;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2254290; DOI=10.1128/jb.172.12.7301-7305.1990;
RA Geoffroy C., Mengaud J., Alouf J.E., Cossart P.;
RT "Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to
RT listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and
RT contains a single cysteine.";
RL J. Bacteriol. 172:7301-7305(1990).
RN [2]
RP PROTEIN SEQUENCE OF 33-60.
RA Alouf J.E., Geoffroy C., Gilles A.M., Falmagne P.;
RL (In) Rappuoli R., Alouf J.E., Falmagne P. (eds.);
RL Bacterial protein toxins, pp.49-50, Gustav Fisher Verlag, Stuttgart (1990).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=6411708; DOI=10.1016/s0021-9258(17)44592-3;
RA Geoffroy C., Alouf J.E.;
RT "Selective purification by thiol-disulfide interchange chromatography of
RT alveolysin, a sulfhydryl-activated toxin of Bacillus alvei. Toxin
RT properties and interaction with cholesterol and liposomes.";
RL J. Biol. Chem. 258:9968-9972(1983).
CC -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by
CC forming pores in cholesterol containing host membranes
CC (PubMed:6411708). After 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 cell membranes, membrane insertion and
CC pore formation; cholesterol binding is mediated by a Thr-Leu pair in
CC the C-terminus. Can be reversibly inactivated by oxidation (By
CC similarity). {ECO:0000250|UniProtKB:P0C2E9,
CC ECO:0000269|PubMed:6411708}.
CC -!- ACTIVITY REGULATION: Inhibited by cholesterol and thiol reagents.
CC {ECO:0000269|PubMed:6411708}.
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:0000269|PubMed:6411708}. Host cell
CC membrane {ECO:0000269|PubMed:6411708}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:6411708}. Note=Secreted as soluble protein that
CC then inserts into the host cell 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; M62709; AAA22224.1; -; Genomic_DNA.
DR PIR; A37858; A37858.
DR AlphaFoldDB; P23564; -.
DR SMR; P23564; -.
DR TCDB; 1.C.12.1.2; the thiol-activated cholesterol-dependent cytolysin (cdc) family.
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 Cytolysis; Direct protein sequencing; Hemolysis; Host cell membrane;
KW Host membrane; Lipid-binding; Membrane; Secreted; Signal; Toxin;
KW Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 33..501
FT /note="Alveolysin"
FT /id="PRO_0000034099"
FT TRANSMEM 191..204
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 211..220
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 289..298
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 306..318
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT MOTIF 460..470
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 492..493
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
FT CONFLICT 56
FT /note="A -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55268 MW; E9A859697E0786CF CRC64;
MKKKSNHLKG RKVLVSLLVS LQVFAFASIS SAAPTEPNDI DMGIAGLNYN RNEVLAIQGD
QISSFVPKEG IQSNGKFIVV ERDKKSLTTS PVDISIVDSI TNRTYPGAIQ LANKDFADNQ
PSLVMAARKP LDISIDLPGL KNENTISVQN PNYGTVSSAI DQLVSTWGEK YSSTHTLPAR
LQYAESMVYS QNQISSALNV NAKVLNGTLG IDFNAVANGE KKVMVAAYKQ IFYTVSAGLP
NNPSDLFDDS VTFAELARKG VSNEAPPLMV SNVAYGRTIY VKLETTSKSN DVQTAFKLLL
NNPSIQASGQ YKDIYENSSF TAVVLGGDAQ THNQVVTKDF NVIQSVIKDN AQFSSKNPAY
PISYTSVFLK DNSIAAVHNN TEYIETKTTE YSKGKIKLDH SGAYVAQFEV YWDEFSYDAD
GQEIVTRKSW DGNWRDRSAH FSTEIPLPPN AKNIRIFARE CTGLAWEWWR TVVDEYNVPL
ASDINVSIWG TTLYPKSSIT H
