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Conserved domains on  [gi|446772973|ref|WP_000850229|]
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MULTISPECIES: hemolytic enterotoxin HBL lytic component L2 [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bacillus_HBL super family cl05388
Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic ...
 35-207 3.45e-42

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.


The actual alignment was detected with superfamily member pfam05791:

Pssm-ID: 461741 [Multi-domain]  Cd Length: 177  Bit Score: 147.12  E-value: 3.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973   35 QQENMDISSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEV------PALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGF 108
Cdd:pfam05791   1 SLGPEGLSEALRKAGSQILLMQAYANTILQQPDVNLSAIknadllSNINQHQKLAKANATYWLNEVKPQLIDTIQNIIGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  109 VTKFNSYYPTLKSFVdNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDGtG 188
Cdd:pfam05791  81 STKFQSYYPTLVEAI-DKGDKADLKEGLTDLQGEIQQNQKNAQQLIEELTDLKLQLAKDSNNFKTDVDTLTSILAGDG-G 158

                         170
                  ....*....|....*....
gi 446772973  189 KIDQLKNEILNTKKAIQND 207
Cdd:pfam05791 159 VIPQLQNEIEDLQGSIKKY 177
ClyA-like super family cl45899
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 42-439 1.02e-20

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).


The actual alignment was detected with superfamily member cd22654:

Pssm-ID: 459244 [Multi-domain]  Cd Length: 333  Bit Score: 92.71  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  42 SSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEVPALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNSYYPTL-- 119
Cdd:cd22654    1 SNSIRSLGSQSPLLQAYALVILKQPNVKIEAMPSLTNHQQTAKENVREWLDEYNPKLIDLNQDMINFSQRFNNYYDKLyd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 120 --KSFVDNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDgTGKIDQLKNEI 197
Cdd:cd22654   81 laGKINEDEQAKEDFLNGINKLQSQLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGS-NGEIAQLRTQI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 198 LNTKKAIQNDLQQIALIPGALNEQGFAIFKEVYSLSKEIIEPaaqagvaaynkgKEINNSILEAekkaaqeateqgktal 277
Cdd:cd22654  160 KTINDEIQEELTKILNRPIEVGDGSINIGKQVFTITITTATT------------KTVDVTSIGG---------------- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 278 eiesakkaareaiekskqgeiaaaaaaktqeydlmkVIDTEKIKKTFGVfaevnkltaeqRAYLDDLEKQNQKIYDLTTK 357
Cdd:cd22654  212 ------------------------------------LINGIGNASDDEV-----------KEAANKIQQKQKELVDLIKK 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 358 LSIADLQKSMLLLTQNDLHTFANQVDVELDLLKRYKEDLNLIKNSITKLSTNVDTTNEQSQ--KDTLRQLKNVISYLEEQ 435
Cdd:cd22654  245 LSDAEIQATQLTLVEDQVNGFTELIKRQIATLENLVEDWEMLNQNMNQLQTNVNSGKIDSKllQKQLKQIKKISDELNKQ 324


                 ....
gi 446772973 436 VYKF 439
Cdd:cd22654  325 TKQF 328
 
Name Accession Description Interval E-value
Bacillus_HBL pfam05791
Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic ...
 35-207 3.45e-42

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: 147.12  E-value: 3.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973   35 QQENMDISSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEV------PALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGF 108
Cdd:pfam05791   1 SLGPEGLSEALRKAGSQILLMQAYANTILQQPDVNLSAIknadllSNINQHQKLAKANATYWLNEVKPQLIDTIQNIIGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  109 VTKFNSYYPTLKSFVdNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDGtG 188
Cdd:pfam05791  81 STKFQSYYPTLVEAI-DKGDKADLKEGLTDLQGEIQQNQKNAQQLIEELTDLKLQLAKDSNNFKTDVDTLTSILAGDG-G 158

                         170
                  ....*....|....*....
gi 446772973  189 KIDQLKNEILNTKKAIQND 207
Cdd:pfam05791 159 VIPQLQNEIEDLQGSIKKY 177
ClyA_NheA-like cd22654
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ...
 42-439 1.02e-20

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: 92.71  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  42 SSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEVPALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNSYYPTL-- 119
Cdd:cd22654    1 SNSIRSLGSQSPLLQAYALVILKQPNVKIEAMPSLTNHQQTAKENVREWLDEYNPKLIDLNQDMINFSQRFNNYYDKLyd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 120 --KSFVDNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDgTGKIDQLKNEI 197
Cdd:cd22654   81 laGKINEDEQAKEDFLNGINKLQSQLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGS-NGEIAQLRTQI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 198 LNTKKAIQNDLQQIALIPGALNEQGFAIFKEVYSLSKEIIEPaaqagvaaynkgKEINNSILEAekkaaqeateqgktal 277
Cdd:cd22654  160 KTINDEIQEELTKILNRPIEVGDGSINIGKQVFTITITTATT------------KTVDVTSIGG---------------- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 278 eiesakkaareaiekskqgeiaaaaaaktqeydlmkVIDTEKIKKTFGVfaevnkltaeqRAYLDDLEKQNQKIYDLTTK 357
Cdd:cd22654  212 ------------------------------------LINGIGNASDDEV-----------KEAANKIQQKQKELVDLIKK 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 358 LSIADLQKSMLLLTQNDLHTFANQVDVELDLLKRYKEDLNLIKNSITKLSTNVDTTNEQSQ--KDTLRQLKNVISYLEEQ 435
Cdd:cd22654  245 LSDAEIQATQLTLVEDQVNGFTELIKRQIATLENLVEDWEMLNQNMNQLQTNVNSGKIDSKllQKQLKQIKKISDELNKQ 324


                 ....
gi 446772973 436 VYKF 439
Cdd:cd22654  325 TKQF 328
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 45-212 1.60e-20

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: 89.78  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  45 LRKLGAQSKLIQTYIDQSLMSPNVQ---LEEVPALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNSYYPTLKS 121
Cdd:cd21116    1 LADLGAASALVQAYVTAILNQPNINlipLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIGYNNTFQSYYPDLIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 122 FVD-----NKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDGT--GKIDQLK 194
Cdd:cd21116   81 LADnlikgDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNAlkNQLNSLA 160

                        170       180
                 ....*....|....*....|.
gi 446772973 195 N---EILNTKKAIQNDLQQIA 212
Cdd:cd21116  161 EqidAAIDALEKLSNDWQTLD 181
 
Name Accession Description Interval E-value
Bacillus_HBL pfam05791
Bacillus haemolytic enterotoxin (HBL); This family consists of several Bacillus haemolytic ...
 35-207 3.45e-42

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: 147.12  E-value: 3.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973   35 QQENMDISSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEV------PALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGF 108
Cdd:pfam05791   1 SLGPEGLSEALRKAGSQILLMQAYANTILQQPDVNLSAIknadllSNINQHQKLAKANATYWLNEVKPQLIDTIQNIIGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  109 VTKFNSYYPTLKSFVdNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDGtG 188
Cdd:pfam05791  81 STKFQSYYPTLVEAI-DKGDKADLKEGLTDLQGEIQQNQKNAQQLIEELTDLKLQLAKDSNNFKTDVDTLTSILAGDG-G 158

                         170
                  ....*....|....*....
gi 446772973  189 KIDQLKNEILNTKKAIQND 207
Cdd:pfam05791 159 VIPQLQNEIEDLQGSIKKY 177
ClyA_NheA-like cd22654
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ...
 42-439 1.02e-20

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: 92.71  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  42 SSSLRKLGAQSKLIQTYIDQSLMSPNVQLEEVPALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNSYYPTL-- 119
Cdd:cd22654    1 SNSIRSLGSQSPLLQAYALVILKQPNVKIEAMPSLTNHQQTAKENVREWLDEYNPKLIDLNQDMINFSQRFNNYYDKLyd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 120 --KSFVDNKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDgTGKIDQLKNEI 197
Cdd:cd22654   81 laGKINEDEQAKEDFLNGINKLQSQLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGS-NGEIAQLRTQI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 198 LNTKKAIQNDLQQIALIPGALNEQGFAIFKEVYSLSKEIIEPaaqagvaaynkgKEINNSILEAekkaaqeateqgktal 277
Cdd:cd22654  160 KTINDEIQEELTKILNRPIEVGDGSINIGKQVFTITITTATT------------KTVDVTSIGG---------------- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 278 eiesakkaareaiekskqgeiaaaaaaktqeydlmkVIDTEKIKKTFGVfaevnkltaeqRAYLDDLEKQNQKIYDLTTK 357
Cdd:cd22654  212 ------------------------------------LINGIGNASDDEV-----------KEAANKIQQKQKELVDLIKK 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 358 LSIADLQKSMLLLTQNDLHTFANQVDVELDLLKRYKEDLNLIKNSITKLSTNVDTTNEQSQ--KDTLRQLKNVISYLEEQ 435
Cdd:cd22654  245 LSDAEIQATQLTLVEDQVNGFTELIKRQIATLENLVEDWEMLNQNMNQLQTNVNSGKIDSKllQKQLKQIKKISDELNKQ 324


                 ....
gi 446772973 436 VYKF 439
Cdd:cd22654  325 TKQF 328
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 45-212 1.60e-20

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: 89.78  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  45 LRKLGAQSKLIQTYIDQSLMSPNVQ---LEEVPALNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNSYYPTLKS 121
Cdd:cd21116    1 LADLGAASALVQAYVTAILNQPNINlipLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIGYNNTFQSYYPDLIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973 122 FVD-----NKEDREGFSDRLEVLQEMAMTNQENAQRQINELTDLKLQLDKKLKDFDTNVATAQGILSTDGT--GKIDQLK 194
Cdd:cd21116   81 LADnlikgDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNAlkNQLNSLA 160

                        170       180
                 ....*....|....*....|.
gi 446772973 195 N---EILNTKKAIQNDLQQIA 212
Cdd:cd21116  161 EqidAAIDALEKLSNDWQTLD 181
ClyA_HblB-like cd22653
Bacillus cereus hemolysin binding component B (HblB), and similar proteins; This model ...
 43-158 2.25e-04

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: 42.58  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446772973  43 SSLRKLGAQSKLIQTYIDQSLMSPNVQLEEVPA--------LNTNQFLIKQDMKEWSSELYPQLILLNSKSKGFVTKFNS 114
Cdd:cd22653    3 EALAKTGSNILVMDLYALTILKQPDINLSGLISidgdlkkkIIQHQETARKNANYWLDTLKPQIIKTNQNIINYNTQFQN 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446772973 115 YYPTLKSFVDNKeDREGFSDRLEVLQEMAMTNQENAQRQINELT 158
Cdd:cd22653   83 YYDTLVDAIDKK-DKETLKEGLTDLYKDISENKKEVDQLIKDLK 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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