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TACY_LISMH
ID   TACY_LISMH              Reviewed;         529 AA.
AC   B8DGM3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Listeriolysin O;
DE   AltName: Full=LLO;
DE   AltName: Full=Thiol-activated cytolysin;
DE   Flags: Precursor;
GN   Name=hly; OrderedLocusNames=LMHCC_2441;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK40776.1; -; Genomic_DNA.
DR   RefSeq; WP_012582095.1; NC_011660.1.
DR   AlphaFoldDB; B8DGM3; -.
DR   SMR; B8DGM3; -.
DR   KEGG; lmh:LMHCC_2441; -.
DR   HOGENOM; CLU_026912_0_0_9; -.
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   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_0000396803"
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   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  58675 MW;  901D20D889C948DE CRC64;
     MKKIMLVFIT LILISLPIAQ QTEAKDASAF NKENSISSMA 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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