MULTISPECIES: HBL/NHE enterotoxin family protein [Bacillus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ClyA_HblB-like | cd22653 | Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ... |
53-366 | 6.25e-78 | |||||
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model includes Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL (HBL), and is a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). HBL is composed of three distinct protein components, B, L1, and L2, which together possess hemolytic, cytotoxic, dermonecrotic, and vascular permeability activities in B. cereus. Although all three HBL components can individually bind to the membrane, it requires the three components to form a complex to form a pore. Structure of HblB shows an elongated, almost entirely alpha-helical protein, except for a short hydrophobic beta-hairpin known as the beta-tongue. HBL from Bacillus toyonensis BV-17 (a strain isolated from feces samples of healthy donors) has antitumor activity both in vitro and in vivo and may have potential as a treatment for colon cancer. For B. toyonesis HBL, combining HBL-B and HBL-L2 had no cytotoxicity but combining HBL-B and HBL-L1 does. : Pssm-ID: 439151 [Multi-domain] Cd Length: 231 Bit Score: 239.41 E-value: 6.25e-78
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| Name | Accession | Description | Interval | E-value | |||||
| ClyA_HblB-like | cd22653 | Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ... |
53-366 | 6.25e-78 | |||||
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model includes Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL (HBL), and is a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). HBL is composed of three distinct protein components, B, L1, and L2, which together possess hemolytic, cytotoxic, dermonecrotic, and vascular permeability activities in B. cereus. Although all three HBL components can individually bind to the membrane, it requires the three components to form a complex to form a pore. Structure of HblB shows an elongated, almost entirely alpha-helical protein, except for a short hydrophobic beta-hairpin known as the beta-tongue. HBL from Bacillus toyonensis BV-17 (a strain isolated from feces samples of healthy donors) has antitumor activity both in vitro and in vivo and may have potential as a treatment for colon cancer. For B. toyonesis HBL, combining HBL-B and HBL-L2 had no cytotoxicity but combining HBL-B and HBL-L1 does. Pssm-ID: 439151 [Multi-domain] Cd Length: 231 Bit Score: 239.41 E-value: 6.25e-78
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| Bacillus_HBL | pfam05791 | Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic ... |
48-215 | 4.07e-38 | |||||
Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic enterotoxins (HblC, HblD, HblA, NheA, and NheB) which can cause food poisoning in humans. Pssm-ID: 461741 [Multi-domain] Cd Length: 177 Bit Score: 134.79 E-value: 4.07e-38
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| Name | Accession | Description | Interval | E-value | |||||
| ClyA_HblB-like | cd22653 | Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ... |
53-366 | 6.25e-78 | |||||
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model includes Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL (HBL), and is a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). HBL is composed of three distinct protein components, B, L1, and L2, which together possess hemolytic, cytotoxic, dermonecrotic, and vascular permeability activities in B. cereus. Although all three HBL components can individually bind to the membrane, it requires the three components to form a complex to form a pore. Structure of HblB shows an elongated, almost entirely alpha-helical protein, except for a short hydrophobic beta-hairpin known as the beta-tongue. HBL from Bacillus toyonensis BV-17 (a strain isolated from feces samples of healthy donors) has antitumor activity both in vitro and in vivo and may have potential as a treatment for colon cancer. For B. toyonesis HBL, combining HBL-B and HBL-L2 had no cytotoxicity but combining HBL-B and HBL-L1 does. Pssm-ID: 439151 [Multi-domain] Cd Length: 231 Bit Score: 239.41 E-value: 6.25e-78
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| Bacillus_HBL | pfam05791 | Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic ... |
48-215 | 4.07e-38 | |||||
Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic enterotoxins (HblC, HblD, HblA, NheA, and NheB) which can cause food poisoning in humans. Pssm-ID: 461741 [Multi-domain] Cd Length: 177 Bit Score: 134.79 E-value: 4.07e-38
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| ClyA_NheA-like | cd22654 | Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
62-322 | 3.11e-31 | |||||
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores. Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 120.83 E-value: 3.11e-31
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| ClyA_Cry6Aa-like | cd22656 | Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
83-365 | 1.00e-20 | |||||
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices. Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 91.28 E-value: 1.00e-20
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| ClyA-like | cd21116 | family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
57-366 | 1.26e-18 | |||||
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA). Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 83.62 E-value: 1.26e-18
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| ClyA_MakA-like | cd22655 | Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
99-373 | 2.55e-17 | |||||
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish. Pssm-ID: 439153 [Multi-domain] Cd Length: 342 Bit Score: 81.94 E-value: 2.55e-17
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| ClyA_AhlB-like | cd22652 | Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes ... |
51-332 | 5.17e-13 | |||||
Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). It consists of three proteins, AhlA, AhlB and AhlC, encoded by one operon containing the three genes. Functional and mutagenic studies support a model of pore assembly where the soluble tetrameric form of AhlC first disassociates into monomers, binds a single membrane leaflet, and then recruits AhlB to promote soluble to pore transition; AhlA then binds to form the active hydrophilic lined pore. The structure of AhlB shows an elongated, almost entirely alpha-helical protein, including a hydrophobic beta-hairpin known as a beta-tongue to shield membrane inserting hydrophobic residues. The head domain of AhlB undergoes a large conformational change involving the beta tongue becoming an extended alpha helix, and the tail domain helices sliding relative to one another as AhlB assembles into a hydrophobic pore. Pssm-ID: 439150 [Multi-domain] Cd Length: 332 Bit Score: 69.17 E-value: 5.17e-13
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| ClyA_XaxA-like | cd22657 | Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ... |
101-366 | 7.05e-08 | |||||
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and similar proteins; This model includes Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, both parts of two-component alpha-helical pore-forming toxins (alpha-PFTs). The xaxAB genes encoding the XaxAB toxin have also been also identified in various plant and human pathogens. XaxAB triggers necrosis and apoptosis in both insect hemocytes and mammalian cells. Structure studies show that component A binds to component B's back, forming a subunit; twelve to fifteen of these subunits then conjoin as the pore-forming toxin. Component A stabilizes each subunit on the membrane and activates component B, which then punctures the membrane by swinging out its lower end. Similarly, Yersinia enterocolitica YaxA, encoded by the yaxAB gene, forms a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Although both subunits bear membrane-active moieties, only YaxA is capable of binding to membranes by itself and YaxB is subsequently recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices; pore formation then progresses by further oligomerization of YaxA-YaxB dimers. YaxAB has been found to be strongly upregulated by the Yersinia master regulator RovA, a transcriptional activator of Yersinia outer membrane protein invasion which is involved in bacterial attachment and invasion across the intestinal epithelium. Pssm-ID: 439155 [Multi-domain] Cd Length: 306 Bit Score: 53.36 E-value: 7.05e-08
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