hly

Zinc metalloproteinase

548 amino acids

Zinc metalloprotease with hemolytic properties.

Belongs to the peptidase M4 family.

56.379 kDa

MKKYYAVTGIALAVGMLCTTQLAGATQAADPSVGSLDSSNVVTEFSAQGNVEQITFKSAIKSAPMSSARSAQTSAIIPGLKNLFVSAPGSDFSLNDSSNNYIKRFTQNIAGIPVLGSSITEVLDGQGAVTSAIGAVTSATKGAFPADLAAGQAAALASATKIASAGKDASAISLVDQKAIWFDAVLIGKGATGSVAVPAYQFSFTTGFAESRVLTVAANDGAILNDRTDRKDINRVVCDANSKVIDLEASNADALLKCGKTQANKPTRIEGQAASSVADVNSVYNFLNDTASFYGANTKANDLTALIGNDEGDGLGKAMRAVVRICVTDSQNGEQCPFANAFWYNGQMTYGQGVTTDDITGHELTHGVTEKTNGLVYANESGAINESMSDVFGEFIDLSNGSSDDTAANRWAIGEGSSLGVIRSMKDPGKYGEPAIYKGSNWKPTATNPNDNNDQGGVHSNSGVGNKLAFLITDGQTFNGQTVTGIGIAKAAQLYWAAQRQLTANATYSSLGKALNSACSANVSNNVAGTTAANCTQVANAIKAVGIK

hly

Halolysin

530 amino acids

Belongs to the peptidase S8 family.

54.703 kDa

MSRDTKRNIGRRSVLKATSALGAFLGLGGVTSATPGRSRSRKKDEIVVGVSDSVSASKATIDSKLPSKATIVHTNETLGYVAVEFPSRASTQARENFKRNVLEADDVEYAEDNATYEAIATPNDPQYGQQYAPQQVNCEAAWDVTYGDPGVTISVVDQGIQYDHEDLEGNMDGSVSNYGDDFVDNDGDPYPVSASENHGTHVGGIAAGGTNNATGHAGISNCSLLSARALGDGGGGSLTDIADAIQWSADQGADVINMSLGGGGFSQTLSNACEYAYNQGSLLVAAAGNGYGNSVSYPAAYDTVMAVSSLDEGETLSAFSNLGPEIELAAPGGNVLSSIPWDNYDTFSGTSMASPVVAGVAGFTLSAHPNLSNAELRSHLQNTAVDVGLSSEEQGHGRVDAGQAVTTDPGDGGGGGDPGDGTCGDETNTETAEGNISSSNPSDAYSYTLDTADPCSATVSLSGPSSADFDLYLTLDGRTPTTSDYDRRSYNWGSDEEISVDLSGNEELGILVNQYSGSGSYTLTIEELGK

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation (By similarity).

Belongs to the thiol-activated cytolysin family.

58.688 kDa

MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation (By similarity).

Belongs to the thiol-activated cytolysin family.

58.688 kDa

MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation (By similarity).

Belongs to the thiol-activated cytolysin family.

58.71 kDa

MKKIMLVFITLILVSLPIAQQTEAKDASAFHKENLISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEINYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNSVDNPIE

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation (By similarity).

Belongs to the thiol-activated cytolysin family.

58.669 kDa

MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENLISSIAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEINYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNSVDNPIE

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation (By similarity).

Belongs to the thiol-activated cytolysin family.

58.675 kDa

MKKIMLVFITLILISLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEINYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNSVDNPIE

hly

Listeriolysin O

529 amino acids

Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome-independent degradation of UBE2I (the SUMO-conjugating enzyme UBC9) and a proteasome-dependent degradation of some sumoylated proteins. Finally, is necessary and sufficient for spacious Listeria-containing phagosomes (SLAPs) formation, suggesting a role for listeriolysin O in promoting L.monocytogenes replication in vacuoles, leading to persistent infection. Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis (PubMed:9284184).

Belongs to the thiol-activated cytolysin family.

58.688 kDa

MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE

hly

Halolysin

519 amino acids

Probable secreted halophilic serine protease showing proteolytic activity toward the protease general substrate azocasein.

Belongs to the peptidase S8 family.

53.516 kDa

MAGTPNFDRRSFLRLAAAAGLTGMAGVTSATPGRSPGPKKDEILVGVTSTADSPRKAVADAVPGNAEIVHENETLSYAAVKFPSKAPKQARENFISAITKRDEVKYAEKNATHEALYTANDPKYGSQYAPQQVNADSAWDTTLGSSSVKIAVVDQGVKYDHPDLSSQFGSNKGRDFVDNDGDPYPDLLSDEYHGTHVAGIAAGTTDNNEGIGGISNSTLLSGRALSESGSGSTSDIADAIEWAADQGADVINLSLGGGGYSSTMKNAVSYATQQGSLVVAAAGNDGRQSVSYPAAYSECVAVSALDPDETLASYSNYGSEIDLAAPGTNVLSCWTTSTEYNEISGTSMATPVVSGVAGLALAVHNLSPADLRNHLKNTAVDIGLSSTKQGSGRVDAANAVTTDPGDGGGGGGGGSKETTYDGTLSSSSDSNCVSHSWNYSSPSQVVIDLSGPSSADFDLYATEGSGTCPTTRSYDYRSWSYDSTEQIVIDNPDTSADLGILVDSYSGSGSYTVTITEKE

hly

Alpha-hemolysin

319 amino acids

Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity).

Belongs to the aerolysin family.

35.973 kDa

MKTRIVSSVTTTLLLGSILMNPVANAADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWIDRSSERYKIDWEKEEMTN

hly

Alpha-hemolysin

319 amino acids

Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis. Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866). Heptamer oligomerization and pore formation is required for lytic activity.

Belongs to the aerolysin family.

35.904 kDa

MKTRIVSSVTTTLLLGSILMNPVAGAADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN

hly

21 kDa hemolysin

194 amino acids

21.219 kDa

MRTRSRSTVRPLWPPPSPARFATWSHYRLRDHGDHTRPVDPRSAGTQVDDEVLEERVAYNLSKDAQLKEEARINVVAYNGKVLLIGQAPTMSASESAKNLAAGAEGVTEIYNEIRTGEKIGVGQISIDSWITTAIKSKLLANSEVKATEVKVITENGEVFLIGKLSPAQADAAAEVARNVRGVNKVIKVINYVQ