TACY_LISSE
ID TACY_LISSE Reviewed; 530 AA.
AC P31830;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Seeligeriolysin {ECO:0000303|PubMed:1543752};
DE Short=LSO;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=lso {ECO:0000303|PubMed:1543752};
OS Listeria seeligeri.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1640;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SLCC;
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).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF PHE-489.
RC STRAIN=ATCC 35967;
RX PubMed=11583846; DOI=10.1111/j.1574-6968.2001.tb10839.x;
RA Ito Y., Kawamura I., Kohda C., Baba H., Kimoto T., Watanabe I., Nomura T.,
RA Mitsuyama M.;
RT "Difference in cholesterol-binding and cytolytic activities between
RT listeriolysin O and seeligeriolysin O: a possible role of alanine residue
RT in tryptophan-rich undecapeptide.";
RL FEMS Microbiol. Lett. 203:185-189(2001).
CC -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by
CC forming pores in cholesterol containing host membranes. L.seeligeri is
CC non-pathogenic, perhaps in part because this protein is about 25% as
CC toxic as listeriolysin O. Mutating a single residue in the
CC undecapeptide increases toxicity 2-fold (PubMed:11583846). After
CC binding to target membranes, the protein undergoes a major conformation
CC change, leading to its insertion in the host membrane and formation of
CC an 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 (By similarity).
CC {ECO:0000250|UniProtKB:P13128, ECO:0000269|PubMed:11583846}.
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 membrane and forms pores formed
CC 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; X60462; CAA42996.1; -; Genomic_DNA.
DR PIR; S22340; S22340.
DR RefSeq; WP_012984716.1; NC_013891.1.
DR AlphaFoldDB; P31830; -.
DR SMR; P31830; -.
DR STRING; 683837.lse_0183; -.
DR GeneID; 32490189; -.
DR eggNOG; ENOG502Z7ST; Bacteria.
DR OMA; NDRTYPG; -.
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; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..530
FT /note="Seeligeriolysin"
FT /id="PRO_0000034103"
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 REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT MUTAGEN 489
FT /note="F->A: Doubles toxicity, increases cholesterol
FT binding about 3.5-fold."
FT /evidence="ECO:0000269|PubMed:11583846"
SQ SEQUENCE 530 AA; 59182 MW; 416F7A4DD2029866 CRC64;
MKIFGLVIMS LLFVSLPITQ QPEARDVPAY DRSEVTISPA ETPESPPATP KTPVEKKHAE
EINKYIWGLN YDKNSILVYQ GEAVTNVPPK KGYKDGSEYI VVEKKKKGIN QNNADISVIN
AISSLTYPGA LVKANRELVE NQPNVLPVKR DSLTLSVDLP GMTKKDNKIF VKNPTKSNVN
NAVNTLVERW NDKYSKAYPN INAKIDYSDE MAYSESQLIA KFGTAFKAVN NSLNVNFEAI
SDGKVQEEVI SFKQIYYNIN VNEPTSPSKF FGGSVTKEQL DALGVNAENP PAYISSVAYG
RQVYVKLSSS SHSNKVKTAF EAAMSGKSVK GDVELTNIIK NSSFKAVIYG GSAKEEVEII
DGNLGELRDI LKKGSTYDRE NPGVPISYTT NFLKDNDLAV VKNNSEYIET TSKSYTDGKI
NIDHSGGYVA QFNISWDEVS YDENGNEIKV HKKWGENYKS KLAHFTSSIY LPGNARNINI
YARECTGLFW EWWRTVIDDR NLPLVKNRNV SIWGTTLYPR HSNNVDNPIQ
