TACY_LISMO
ID TACY_LISMO Reviewed; 529 AA.
AC P13128; Q48747; Q57096; Q57206;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Listeriolysin O {ECO:0000303|PubMed:3110067};
DE AltName: Full=LLO;
DE AltName: Full=Thiol-activated cytolysin;
DE Flags: Precursor;
GN Name=hly; Synonyms=hlyA, lisA; OrderedLocusNames=lmo0202;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=2505236; DOI=10.1093/nar/17.15.6406;
RA Domann E., Chakraborty T.;
RT "Nucleotide sequence of the listeriolysin gene from a Listeria
RT monocytogenes serotype 1/2a strain.";
RL Nucleic Acids Res. 17:6406-6406(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3126142; DOI=10.1128/iai.56.4.766-772.1988;
RA Mengaud J., Vicente M.-F., Chenevert J., Pereira J.M., Geoffroy C.,
RA Gicquel-Sanzey B., Baquero F., Perez-Diaz J.-C., Cossart P.;
RT "Expression in Escherichia coli and sequence analysis of the listeriolysin
RT O determinant of Listeria monocytogenes.";
RL Infect. Immun. 56:766-772(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=12067;
RX PubMed=1937753; DOI=10.1128/iai.59.11.3945-3951.1991;
RA Rasmussen O.F., Beck T., Olsen J.E., Dons L., Rossen L.;
RT "Listeria monocytogenes isolates can be classified into two major types
RT according to the sequence of the listeriolysin gene.";
RL Infect. Immun. 59:3945-3951(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F4233 / Serotype 1/2b, F5782 / Serotype 4b, and
RC F6789 / Serotype 1/2b;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 413-480.
RX PubMed=2824384; DOI=10.1128/iai.55.12.3225-3227.1987;
RA Mengaud J., Chenevert J., Geoffroy C., Gaillard J.-L., Cossart P.;
RT "Identification of the structural gene encoding the SH-activated hemolysin
RT of Listeria monocytogenes: listeriolysin O is homologous to streptolysin O
RT and pneumolysin.";
RL Infect. Immun. 55:3225-3227(1987).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=3110067; DOI=10.1128/iai.55.7.1641-1646.1987;
RA Geoffroy C., Gaillard J.L., Alouf J.E., Berche P.;
RT "Purification, characterization, and toxicity of the sulfhydryl-activated
RT hemolysin listeriolysin O from Listeria monocytogenes.";
RL Infect. Immun. 55:1641-1646(1987).
RN [8]
RP MUTAGENESIS OF CYS-484; TRP-491 AND TRP-492.
RX PubMed=1965218; DOI=10.1111/j.1365-2958.1990.tb00578.x;
RA Michel E., Reich K.A., Favier R., Berche P., Cossart P.;
RT "Attenuated mutants of the intracellular bacterium Listeria monocytogenes
RT obtained by single amino acid substitutions in listeriolysin O.";
RL Mol. Microbiol. 4:2167-2178(1990).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF CYS-484; TRP-491 AND TRP-492.
RC STRAIN=SLCC 5764 / Serovar 1/2a;
RX PubMed=8675352; DOI=10.1128/iai.64.6.2359-2361.1996;
RA Tang P., Rosenshine I., Cossart P., Finlay B.B.;
RT "Listeriolysin O activates mitogen-activated protein kinase in eucaryotic
RT cells.";
RL Infect. Immun. 64:2359-2361(1996).
RN [10]
RP ANTIGENICITY.
RX PubMed=9284184; DOI=10.1128/iai.65.9.3976-3980.1997;
RA Grenningloh R., Darji A., Wehland J., Chakraborty T., Weiss S.;
RT "Listeriolysin and IrpA are major protein targets of the human humoral
RT response against Listeria monocytogenes.";
RL Infect. Immun. 65:3976-3980(1997).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=9314564; DOI=10.1084/jem.186.7.1159;
RA Beauregard K.E., Lee K.D., Collier R.J., Swanson J.A.;
RT "pH-dependent perforation of macrophage phagosomes by listeriolysin O from
RT Listeria monocytogenes.";
RL J. Exp. Med. 186:1159-1163(1997).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ALA-488.
RC STRAIN=EGD;
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).
RN [13]
RP DOMAIN.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=11251831; DOI=10.1111/j.1365-2958.2001.02281.x;
RA Lety M.A., Frehel C., Dubail I., Beretti J.L., Kayal S., Berche P.,
RA Charbit A.;
RT "Identification of a PEST-like motif in listeriolysin O required for
RT phagosomal escape and for virulence in Listeria monocytogenes.";
RL Mol. Microbiol. 39:1124-1139(2001).
RN [14]
RP FUNCTION, REGULATION BY PH, AND MUTAGENESIS OF LEU-461.
RC STRAIN=10403S / Serovar 1/2a;
RX PubMed=11901168; DOI=10.1083/jcb.200201081;
RA Glomski I.J., Gedde M.M., Tsang A.W., Swanson J.A., Portnoy D.A.;
RT "The Listeria monocytogenes hemolysin has an acidic pH optimum to
RT compartmentalize activity and prevent damage to infected host cells.";
RL J. Cell Biol. 156:1029-1038(2002).
RN [15]
RP DOMAIN, AND MUTAGENESIS OF PRO-49; LYS-50 AND PRO-52.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=12406215; DOI=10.1046/j.1365-2958.2002.03176.x;
RA Lety M.A., Frehel C., Berche P., Charbit A.;
RT "Critical role of the N-terminal residues of listeriolysin O in phagosomal
RT escape and virulence of Listeria monocytogenes.";
RL Mol. Microbiol. 46:367-379(2002).
RN [16]
RP PHOSPHORYLATION AT SER-44, UBIQUITINATION, DOMAIN, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF SER-44.
RC STRAIN=10403S / Serovar 1/2a;
RX PubMed=16441444; DOI=10.1111/j.1462-5822.2005.00631.x;
RA Schnupf P., Portnoy D.A., Decatur A.L.;
RT "Phosphorylation, ubiquitination and degradation of listeriolysin O in
RT mammalian cells: role of the PEST-like sequence.";
RL Cell. Microbiol. 8:353-364(2006).
RN [17]
RP ACTIVITY REGULATION.
RC STRAIN=10403S / Serovar 1/2a;
RX PubMed=16859495; DOI=10.1111/j.1365-2958.2006.05286.x;
RA Schnupf P., Hofmann J., Norseen J., Glomski I.J., Schwartzstein H.,
RA Decatur A.L.;
RT "Regulated translation of listeriolysin O controls virulence of Listeria
RT monocytogenes.";
RL Mol. Microbiol. 61:999-1012(2006).
RN [18]
RP REVIEW.
RX PubMed=17720603; DOI=10.1016/j.micinf.2007.05.005;
RA Schnupf P., Portnoy D.A.;
RT "Listeriolysin O: a phagosome-specific lysin.";
RL Microbes Infect. 9:1176-1187(2007).
RN [19]
RP FUNCTION IN SLAPS FORMATION.
RC STRAIN=10403S / Serovar 1/2a;
RX PubMed=18202661; DOI=10.1038/nature06479;
RA Birmingham C.L., Canadien V., Kaniuk N.A., Steinberg B.E., Higgins D.E.,
RA Brumell J.H.;
RT "Listeriolysin O allows Listeria monocytogenes replication in macrophage
RT vacuoles.";
RL Nature 451:350-354(2008).
RN [20]
RP FUNCTION.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=20414307; DOI=10.1038/nature08963;
RA Ribet D., Hamon M., Gouin E., Nahori M.A., Impens F., Neyret-Kahn H.,
RA Gevaert K., Vandekerckhove J., Dejean A., Cossart P.;
RT "Listeria monocytogenes impairs SUMOylation for efficient infection.";
RL Nature 464:1192-1195(2010).
RN [21]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000303|PubMed:21844299};
RX PubMed=21844299; DOI=10.1093/infdis/jir396;
RA Aubry C., Goulard C., Nahori M.A., Cayet N., Decalf J., Sachse M.,
RA Boneca I.G., Cossart P., Dussurget O.;
RT "OatA, a peptidoglycan O-acetyltransferase involved in Listeria
RT monocytogenes immune escape, is critical for virulence.";
RL J. Infect. Dis. 204:731-740(2011).
RN [22] {ECO:0007744|PDB:4CDB}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 39-526, FUNCTION, PROBABLE
RP OLIGOMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 38-SER--PRO-52;
RP ALA-40; SER-44; LYS-175; SER-176; ASN-230; GLU-262 AND ASP-394.
RX PubMed=24751541; DOI=10.1038/ncomms4690;
RA Koester S., van Pee K., Hudel M., Leustik M., Rhinow D., Kuehlbrandt W.,
RA Chakraborty T., Yildiz O.;
RT "Crystal structure of listeriolysin O reveals molecular details of
RT oligomerization and pore formation.";
RL Nat. Commun. 5:3690-3690(2014).
CC -!- FUNCTION: A cholesterol-dependent pore-forming toxin, which is a major
CC virulence factor required for the escape of bacteria from phagosomal
CC vacuoles and entry into the host cytosol. 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. Listeriolysin O activates mitogen-activated protein (MAP)
CC kinase activity in host cells, most likely as a result of the
CC permeabilization of the host cell membrane. Also induces a proteasome-
CC independent degradation of UBE2I (the SUMO-conjugating enzyme UBC9) and
CC a proteasome-dependent degradation of some sumoylated proteins.
CC Finally, is necessary and sufficient for spacious Listeria-containing
CC phagosomes (SLAPs) formation, suggesting a role for listeriolysin O in
CC promoting L.monocytogenes replication in vacuoles, leading to
CC persistent infection. Recognized by serum from healthy humans exposed
CC to L.monocytogenes as well from patients who have recovered from
CC listeriosis (PubMed:9284184). {ECO:0000269|PubMed:11583846,
CC ECO:0000269|PubMed:11901168, ECO:0000269|PubMed:18202661,
CC ECO:0000269|PubMed:20414307, ECO:0000269|PubMed:24751541,
CC ECO:0000269|PubMed:3110067, ECO:0000269|PubMed:8675352,
CC ECO:0000269|PubMed:9284184}.
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. Multiple regulatory mechanisms include translational
CC repression, which is required to minimize levels of listeriolysin O in
CC the host cytosol. In addition, cytolytic activity is pH-dependent.
CC Activity is high in the acidic environment of the phagosome and is
CC turned off in the neutral pH of the cytosol. Listeriolysin O is also
CC ubiquitinated and rapidly degraded by host proteasome in cytosol. The
CC lytic activity is activated by reducing agents and suppressed by
CC oxidation. Also inhibited by very low amounts of cholesterol.
CC {ECO:0000269|PubMed:16441444, ECO:0000269|PubMed:16859495,
CC ECO:0000269|PubMed:3110067, ECO:0000269|PubMed:9314564}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Cytolytic activity is undetectable at pH 7.0.
CC {ECO:0000269|PubMed:3110067};
CC -!- SUBUNIT: Homooligomeric pore complex of 35-50 subunits; when inserted
CC in the host membrane. {ECO:0000305|PubMed:24751541}.
CC -!- INTERACTION:
CC P13128; P13128: hly; NbExp=4; IntAct=EBI-6407357, EBI-6407357;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24751541,
CC ECO:0000269|PubMed:3110067}. Host membrane
CC {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:3110067}. Host cell membrane
CC {ECO:0000269|PubMed:3110067}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:3110067}. Note=Secreted as soluble protein that
CC then inserts into the host membrane and forms pores formed by
CC transmembrane beta-strands. {ECO:0000305|PubMed:24751541}.
CC -!- DOMAIN: The N-terminal region is not required for secretion and
CC hemolytic activity, but is involved in phagosomal escape of bacteria in
CC infected cells and is critical for bacterial virulence. This region
CC contains a PEST-like sequence, which does not mediate proteasomal
CC degradation, but controls listeriolysin O production in the cytosol.
CC {ECO:0000269|PubMed:11251831, ECO:0000269|PubMed:12406215,
CC ECO:0000269|PubMed:16441444}.
CC -!- PTM: Phosphorylated. Phosphorylation does not appear to be required for
CC ubiquitination or degradation. {ECO:0000269|PubMed:16441444}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16441444}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have severely reduced
CC cytokine production in the mouse Listeria-infected liver cells compared
CC to wild-type. {ECO:0000269|PubMed:21844299}.
CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69528.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA69531.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X15127; CAA33223.1; -; Genomic_DNA.
DR EMBL; M24199; AAA03018.1; -; Unassigned_DNA.
DR EMBL; X60035; CAA42639.1; -; Genomic_DNA.
DR EMBL; U25446; AAA69528.1; ALT_INIT; Genomic_DNA.
DR EMBL; U25449; AAA69531.1; ALT_INIT; Genomic_DNA.
DR EMBL; U25452; AAA69534.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00729.1; -; Genomic_DNA.
DR PIR; A43505; A43505.
DR PIR; AC1100; AC1100.
DR PIR; S24231; S24231.
DR RefSeq; NP_463733.1; NC_003210.1.
DR RefSeq; WP_003722731.1; NZ_CP023861.1.
DR PDB; 4CDB; X-ray; 2.15 A; A=39-526.
DR PDBsum; 4CDB; -.
DR AlphaFoldDB; P13128; -.
DR SMR; P13128; -.
DR IntAct; P13128; 1.
DR MINT; P13128; -.
DR STRING; 169963.lmo0202; -.
DR TCDB; 1.C.12.1.7; the thiol-activated cholesterol-dependent cytolysin (cdc) family.
DR iPTMnet; P13128; -.
DR PaxDb; P13128; -.
DR EnsemblBacteria; CAD00729; CAD00729; CAD00729.
DR GeneID; 987033; -.
DR KEGG; lmo:lmo0202; -.
DR PATRIC; fig|169963.11.peg.207; -.
DR eggNOG; ENOG502Z7ST; Bacteria.
DR HOGENOM; CLU_026912_0_0_9; -.
DR OMA; NDRTYPG; -.
DR BioCyc; LMON169963:LMO0202-MON; -.
DR PHI-base; PHI:6618; -.
DR PHI-base; PHI:7897; -.
DR Proteomes; UP000000817; 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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Cytolysis; Hemolysis; Host cell membrane; Host membrane;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Toxin; Transmembrane; Transmembrane beta strand; Ubl conjugation;
KW Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..529
FT /note="Listeriolysin O"
FT /id="PRO_0000034102"
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"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:16441444"
FT VARIANT 35
FT /note="S -> L (in strain: F4233 / Serotype 1/2b, F5782 /
FT Serotype 4b, F6789 / Serotype 1/2b and 12067)"
FT VARIANT 438
FT /note="V -> I (in strain: F4233 / Serotype 1/2b, F5782 /
FT Serotype 4b, F6789 / Serotype 1/2b and 12067)"
FT VARIANT 523
FT /note="K -> S (in strain: F4233 / Serotype 1/2b, F5782 /
FT Serotype 4b, F6789 / Serotype 1/2b and 12067)"
FT MUTAGEN 38..52
FT /note="Missing: 2.5-fold increase in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 40
FT /note="A->W: 2.5-fold increase in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 44
FT /note="S->A: 1500-fold decrease in virulence."
FT /evidence="ECO:0000269|PubMed:16441444"
FT MUTAGEN 44
FT /note="S->D,E: 2-fold increase in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 49
FT /note="P->A: Does not affect secretion and hemolytic
FT activity. No defect in phagosomal escape. Shows a clear
FT attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:12406215"
FT MUTAGEN 50
FT /note="K->A: Does not affect secretion and hemolytic
FT activity. Slight decrease in phagosomal escape. Shows a
FT clear attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:12406215"
FT MUTAGEN 52
FT /note="P->A: Does not affect secretion and hemolytic
FT activity. Slight decrease in phagosomal escape. Shows a
FT clear attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:12406215"
FT MUTAGEN 175
FT /note="K->E: Loss of hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 176
FT /note="S->W: Loss of hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 230
FT /note="N->W: 50% hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 262
FT /note="E->K: Loss of hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 262
FT /note="E->W: No change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 394
FT /note="D->W: 3-fold increase in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:24751541"
FT MUTAGEN 461
FT /note="L->T: 10-fold increase in hemolytic activity at
FT neutral pH, but 100-fold decrease in virulence."
FT /evidence="ECO:0000269|PubMed:11901168"
FT MUTAGEN 484
FT /note="C->A: 25% decrease in hemolytic activity, but still
FT able to stimulate MAP kinase tyrosine phosphorylation in
FT host cells. Does not affect membrane-binding capacity."
FT /evidence="ECO:0000269|PubMed:1965218,
FT ECO:0000269|PubMed:8675352"
FT MUTAGEN 484
FT /note="C->S: 80% decrease in hemolytic activity, but still
FT able to stimulate MAP kinase tyrosine phosphorylation in
FT host cells. Does not affect membrane-binding capacity."
FT /evidence="ECO:0000269|PubMed:1965218,
FT ECO:0000269|PubMed:8675352"
FT MUTAGEN 488
FT /note="A->F: Decreases toxicity by about 40%, decreases
FT cholesterol binding by 25%."
FT /evidence="ECO:0000269|PubMed:11583846"
FT MUTAGEN 491
FT /note="W->A: 95% decrease in hemolytic activity and no
FT stimulation of MAP kinase activity. Does not affect
FT membrane-binding capacity."
FT /evidence="ECO:0000269|PubMed:1965218,
FT ECO:0000269|PubMed:8675352"
FT MUTAGEN 492
FT /note="W->A: 99.9% decrease in hemolytic activity and no
FT stimulation of MAP kinase activity. Does not affect
FT membrane-binding capacity."
FT /evidence="ECO:0000269|PubMed:1965218,
FT ECO:0000269|PubMed:8675352"
SQ SEQUENCE 529 AA; 58688 MW; 83B6B0C11C033FB1 CRC64;
MKKIMLVFIT LILVSLPIAQ 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 FNISWDEVNY DPEGNEIVQH KNWSENNKSK LAHFTSSIYL PGNARNINVY
AKECTGLAWE WWRTVIDDRN LPLVKNRNIS IWGTTLYPKY SNKVDNPIE
