TACY_CLOP1
ID TACY_CLOP1 Reviewed; 500 AA.
AC Q0TUS0; P19995;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Perfringolysin O;
DE Short=PFO;
DE AltName: Full=Theta-toxin;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=pfo; Synonyms=pfoA, pfoR; OrderedLocusNames=CPF_0156;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-44.
RX PubMed=2903128; DOI=10.1128/iai.56.12.3235-3240.1988;
RA Tweten R.K.;
RT "Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from
RT Clostridium perfringens: significant homology with the genes for
RT streptolysin O and pneumolysin.";
RL Infect. Immun. 56:3235-3240(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 492-500.
RX PubMed=8577281; DOI=10.1111/j.1348-0421.1995.tb03256.x;
RA Shimizu T., Kobayashi T., Ba-Thein W., Ohtani K., Hayashi H.;
RT "Sequence analysis of flanking regions of the pfoA gene of Clostridium
RT perfringens: beta-galactosidase gene (pbg) is located in the 3'-flanking
RT region.";
RL Microbiol. Immunol. 39:677-686(1995).
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 assembles into a pre-pore complex. A
CC conformation change leads to insertion in the host membrane and
CC formation of an oligomeric pore complex. Cholesterol is required for
CC binding to host cell membranes, membrane insertion and pore formation;
CC cholesterol binding is mediated by a Thr-Leu pair in the C-terminus.
CC Can be reversibly inactivated by oxidation.
CC {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 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 huge
CC pores formed by transmembrane beta-strands.
CC {ECO:0000250|UniProtKB:Q04IN8}.
CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC {ECO:0000305}.
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DR EMBL; M36704; AAA23270.1; -; Genomic_DNA.
DR EMBL; CP000246; ABG82518.1; -; Genomic_DNA.
DR EMBL; D49537; BAA08481.1; -; Genomic_DNA.
DR PIR; B43577; B43577.
DR RefSeq; WP_003462918.1; NC_008261.1.
DR AlphaFoldDB; Q0TUS0; -.
DR SMR; Q0TUS0; -.
DR STRING; 195103.CPF_0156; -.
DR EnsemblBacteria; ABG82518; ABG82518; CPF_0156.
DR GeneID; 29572721; -.
DR KEGG; cpf:CPF_0156; -.
DR eggNOG; ENOG502Z7ST; Bacteria.
DR HOGENOM; CLU_026912_1_0_9; -.
DR OMA; NDRTYPG; -.
DR OrthoDB; 1219984at2; -.
DR Proteomes; UP000001823; 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 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..28
FT /evidence="ECO:0000269|PubMed:2903128"
FT CHAIN 29..500
FT /note="Perfringolysin O"
FT /id="PRO_0000273630"
FT TRANSMEM 189..202
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 209..218
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 287..296
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 304..316
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT MOTIF 458..468
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 490..491
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
FT CONFLICT 126..128
FT /note="RKP -> EA (in Ref. 1; AAA23270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55800 MW; 5286E9AF38EF8EF0 CRC64;
MIRFKKTKLI ASIAMALCLF SQPVISFSKD ITDKNQSIDS GISSLSYNRN EVLASNGDKI
ESFVPKEGKK AGNKFIVVER QKRSLTTSPV DISIIDSVND RTYPGALQLA DKAFVENRPT
ILMVKRKPIN INIDLPGLKG ENSIKVDDPT YGKVSGAIDE LVSKWNEKYS STHTLPARTQ
YSESMVYSKS QISSALNVNA KVLENSLGVD FNAVANNEKK VMILAYKQIF YTVSADLPKN
PSDLFDDSVT FNDLKQKGVS NEAPPLMVSN VAYGRTIYVK LETTSSSKDV QAAFKALIKN
TDIKNSQQYK DIYENSSFTA VVLGGDAQEH NKVVTKDFDE IRKVIKDNAT FSTKNPAYPI
SYTSVFLKDN SVAAVHNKTD YIETTSTEYS KGKINLDHSG AYVAQFEVAW DEVSYDKEGN
EVLTHKTWDG NYQDKTAHYS TVIPLEANAR NIRIKARECT GLAWEWWRDV ISEYDVPLTN
NINVSIWGTT LYPGSSITYN
