(data stored in ACNUC10821 zone)

SWISSPROT: TACY_LISMF

ID   TACY_LISMF              Reviewed;         529 AA.
AC   Q724L1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Listeriolysin O;
DE   AltName: Full=LLO;
DE   AltName: Full=Thiol-activated cytolysin;
DE   Flags: Precursor;
GN   Name=hly; OrderedLocusNames=LMOf2365_0213;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9541569; DOI=10.1007/s002849900315;
RA   Vines A., Swaminathan B.;
RT   "Identification and characterization of nucleotide sequence differences in
RT   three virulence-associated genes of Listeria monocytogenes strains
RT   representing clinically important serotypes.";
RL   Curr. Microbiol. 36:309-318(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Sulfhydryl-activated toxin that causes cytolysis by forming
CC       pores in cholesterol containing host membranes. After binding to target
CC       membranes, the protein undergoes a major conformation change, leading
CC       to its insertion in the host membrane and formation of an oligomeric
CC       pore complex. Cholesterol may be required for binding to host
CC       membranes, membrane insertion and pore formation. 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomeric pore complex; when inserted in the host
CC       membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host cell
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC       Note=Secreted as soluble protein that then inserts into the host
CC       membrane and forms pores formed by transmembrane beta-strands.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiol-activated cytolysin family.
CC       {ECO:0000305}.
DR   EMBL; U25443; AAA69525.1; -; Genomic_DNA.
DR   EMBL; AE017262; AAT03000.1; -; Genomic_DNA.
DR   RefSeq; WP_010958688.1; NC_002973.6.
DR   SMR; Q724L1; -.
DR   PRIDE; Q724L1; -.
DR   EnsemblBacteria; AAT03000; AAT03000; LMOf2365_0213.
DR   KEGG; lmf:LMOf2365_0213; -.
DR   KO; K11031; -.
DR   OMA; NDRTYPG; -.
DR   BioCyc; LMON265669:G1G0V-212-MONOMER; -.
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; ISS:JCVI.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; ISS:JCVI.
DR   GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:JCVI.
DR   GO; GO:0009405; P:pathogenesis; ISS:JCVI.
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;
DR   PRODOM; Q724L1.
DR   SWISS-2DPAGE; Q724L1.
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_0000034101"
FT   SITE            484
FT                   /note="Binding to cholesterol"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   529 AA;  58669 MW;  F6C64CE10DB2363E CRC64;
     MKKIMLVFIT LILVSLPIAQ QTEAKDASAF NKENLISSIA 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
//

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