TACY_LISMC
ID TACY_LISMC Reviewed; 529 AA.
AC C1KYD5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Listeriolysin O;
DE AltName: Full=LLO;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=hly; OrderedLocusNames=Lm4b_00200;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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 undergoes a major conformation change,
CC leading to its insertion in the host membrane and formation of an
CC 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. Acts as major
CC virulence factor required for the escape of bacteria from phagosomal
CC vacuoles and entry into the host cytosol. Can be reversibly inactivated
CC by oxidation. {ECO:0000250|UniProtKB:P13128}.
CC -!- ACTIVITY REGULATION: Activity of listeriolysin O is regulated on
CC multiple levels. It should be high in the phagosome, thereby allowing
CC escape of the bacteria from the phagosomal compartment. Then, once
CC inside the host cytosol, the activity must be controlled to prevent
CC lysis of the host plasma membrane and loss of the intracellular
CC environment. {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 membrane {ECO:0000250|UniProtKB:P13128}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04IN8}. Host cell membrane
CC {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 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; FM242711; CAS03990.1; -; Genomic_DNA.
DR RefSeq; WP_003740376.1; NC_012488.1.
DR AlphaFoldDB; C1KYD5; -.
DR SMR; C1KYD5; -.
DR KEGG; lmc:Lm4b_00200; -.
DR HOGENOM; CLU_026912_0_0_9; -.
DR OMA; NDRTYPG; -.
DR BioCyc; LMON568819:LM4B_RS01010-MON; -.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..529
FT /note="Listeriolysin O"
FT /id="PRO_0000396802"
FT TRANSMEM 214..227
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 234..243
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 312..321
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 329..341
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT MOTIF 483..493
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 515..516
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
SQ SEQUENCE 529 AA; 58710 MW; 31DA3D795D253F4E CRC64;
MKKIMLVFIT LILVSLPIAQ QTEAKDASAF HKENLISSMA PPASPPASPK TPIEKKHADE
IDKYIQGLDY NKNNVLVYHG DAVTNVPPRK GYKDGNEYIV VEKKKKSINQ NNADIQVVNA
ISSLTYPGAL VKANSELVEN QPDVLPVKRD SLTLSIDLPG MTNQDNKIVV KNATKSNVNN
AVNTLVERWN EKYAQAYPNV SAKIDYDDEM AYSESQLIAK FGTAFKAVNN SLNVNFGAIS
EGKMQEEVIS FKQIYYNVNV NEPTRPSRFF GKAVTKEQLQ ALGVNAENPP AYISSVAYGR
QVYLKLSTNS HSTKVKAAFD AAVSGKSVSG DVELTNIIKN SSFKAVIYGG SAKDEVQIID
GNLGDLRDIL KKGATFNRET PGVPIAYTTN FLKDNELAVI KNNSEYIETT SKAYTDGKIN
IDHSGGYVAQ FNISWDEINY DPEGNEIVQH KNWSENNKSK LAHFTSSIYL PGNARNINVY
AKECTGLAWE WWRTVIDDRN LPLVKNRNIS IWGTTLYPKY SNSVDNPIE
