TACY_CLOTE
ID TACY_CLOTE Reviewed; 527 AA.
AC Q893D9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tetanolysin {ECO:0000303|PubMed:6997696};
DE AltName: Full=Tetanolysin O {ECO:0000303|PubMed:12552129};
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN OrderedLocusNames=CTC_01888;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
RN [2]
RP FUNCTION AS A TOXIN, ACTIVITY REGULATION, PURIFICATION, SUBCELLULAR
RP LOCATION, AND POST-TRANSLATIONAL MODIFICATION.
RC STRAIN=Harvard A-47;
RX PubMed=6997696; DOI=10.1111/j.1348-0421.1980.tb02860.x;
RA Mitsui N., Mitsui K., Hase J.;
RT "Purification and some properties of tetanolysin.";
RL Microbiol. Immunol. 24:575-584(1980).
CC -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by
CC forming pores in cholesterol-containing host membranes
CC (PubMed:6997696). 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 membranes, membrane insertion and pore
CC formation; cholesterol binding is mediated by a Thr-Leu pair in the C-
CC terminus (By similarity). {ECO:0000250|UniProtKB:P13128,
CC ECO:0000250|UniProtKB:Q04IN8, ECO:0000269|PubMed:6997696}.
CC -!- ACTIVITY REGULATION: Cytolysis of host cells is inhibited by
CC cholesterol. {ECO:0000269|PubMed:6997696}.
CC -!- SUBUNIT: Homooligomeric pore complex containing 35-50 subunits; when
CC inserted in the host membrane. {ECO:0000250|UniProtKB:Q04IN8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6997696}. Host cell
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 cell membrane and forms huge pores formed by
CC transmembrane beta-strands. {ECO:0000250|UniProtKB:Q04IN8}.
CC -!- PTM: Purified 48 and 53 kDa proteins with 4 different pIs (6.1, 5.6,
CC 5.3 and 6.6) in decreasing order of activity.
CC {ECO:0000269|PubMed:6997696}.
CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC {ECO:0000305}.
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DR EMBL; AE015927; AAO36403.1; -; Genomic_DNA.
DR RefSeq; WP_011100063.1; NC_004557.1.
DR AlphaFoldDB; Q893D9; -.
DR SMR; Q893D9; -.
DR STRING; 212717.CTC_01888; -.
DR EnsemblBacteria; AAO36403; AAO36403; CTC_01888.
DR GeneID; 64179205; -.
DR KEGG; ctc:CTC_01888; -.
DR HOGENOM; CLU_026912_1_0_9; -.
DR OMA; NDRTYPG; -.
DR OrthoDB; 1219984at2; -.
DR Proteomes; UP000001412; 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; Hemolysis; Host cell membrane; Host membrane; Lipid-binding;
KW Membrane; Reference proteome; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..527
FT /note="Tetanolysin"
FT /id="PRO_5009737782"
FT TRANSMEM 215..228
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 235..244
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 313..322
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 330..342
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT MOTIF 484..494
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 516..517
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
SQ SEQUENCE 527 AA; 59077 MW; BED1BD1D9EA857C0 CRC64;
MNKNVLKFVS RSLLIFSMTG LISNYNSSNV LAKGNVEEHS LINNGQVVTS NTKCNLAKDN
SSDIDKNIYG LSYDPRKILS YNGEQVENFV PAEGFENPDK FIVVKREKKS ISDSTADISI
IDSINDRTYP GAIQLANRNL MENKPDIISC ERKPITISVD LPGMAEDGKK VVNSPTYSSV
NSAINSILDT WNSKYSSKYT IPTRMSYSDT MVYSQSQLSA AVGCNFKALN KALNIDFDSI
FKGEKKVMLL AYKQIFYTVS VDPPNRPSDL FGDSVTFDEL ALKGINNNNP PAYVSNVAYG
RTIYVKLETT SKSSHVKAAF KALINNQDIS SNAEYKDILN QSSFTATVLG GGAQEHNKII
TKDFDEIRNI IKNNSVYSPQ NPGYPISYTT TFLKDNSIAS VNNKTEYIET TATEYTNGKI
VLDHSGAYVA QFQVTWDEVS YDEKGNEIVE HKAWEGNNRD RTAHFNTEIY LKGNARNISV
KIRECTGLAW EWWRTIVDVK NIPLAKERTF YIWGTTLYPK TSIETKM
