1.C.4.2.1 α-Toxin forms large ion permeable (slightly anion-selective) pores with no lipid specificity. It induces rapid cell necrosis in many cell types (Knapp et al., 2009). The structure of the membrane-spanning domain has been solved (Melton et al. 2004).
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Accession Number: | Q53482 |
Protein Name: | Alpha-toxin |
Length: | 443 |
Molecular Weight: | 49786.00 |
Species: | Clostridium septicum [1504] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Secreted1 |
Substrate |
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Pfam: |
PF01117
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[1] “The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin.” Ballard J. et.al. 7806374
[2] “Cloning, nucleotide sequence and expression of a hemolysin gene of Clostridium septicum.” Imagawa T. et.al. 8200504
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1: MSKKSFAKKV ICTSMIAIQC AAVVPHVQAY ALTNLEEGGY ANHNNASSIK IFGYEDNEDL
61: KAKIIQDPEF IRNWANVAHS LGFGWCGGTA NPNVGQGFEF KREVGAGGKV SYLLSARYNP
121: NDPYASGYRA KDRLSMKISN VRFVIDNDSI KLGTPKVKKL APLNSASFDL INESKTESKL
181: SKTFNYTTSK TVSKTDNFKF GEKIGVKTSF KVGLEAIADS KVETSFEFNA EQGWSNTNST
241: TETKQESTTY TATVSPQTKK RLFLDVLGSQ IDIPYEGKIY MEYDIELMGF LRYTGNARED
301: HTEDRPTVKL KFGKNGMSAE EHLKDLYSHK NINGYSEWDW KWVDEKFGYL FKNSYDALTS
361: RKLGGIIKGS FTNINGTKIV IREGKEIPLP DKKRRGKRSV DSLDARLQNE GIRIENIETQ
421: DVPGFRLNSI TYNDKKLILI NNI