1.C.72.4.1 Heat labile enterotoxin AB, EltAB, ItpAB, ToxAB, LT-AB, cholera toxin (258 aas and 124 aas, respectively). The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. The A2 domain of LTA has cell penitration function (Liu et al. 2016). LT holotoxin can enter intestinal epithelial cells and cause diarrhea. The A2 domain might be
useful as a transport vehicle for other proteins (Liu et al. 2016). A biotinylated cholera toxin becomes a fusogenic
lectin upon cross-linking with streptavidin. This reengineered
protein brings about hemifusion and fusion of vesicles as demonstrated
by mixing of fluorescently labeled lipids between vesicles as well as
content mixing of liposomes filled with fluorescently labeled dextran (Wehrum et al. 2022).
|
Accession Number: | P43530 |
Protein Name: | Heat-labile enterotoxin A chain |
Length: | 258 |
Molecular Weight: | 29872.00 |
Species: | Escherichia coli O78:H11 (strain H10407 / ETEC) [316401] |
Substrate |
toxin |
---|
1: MKNITFIFFI LLASPLYANG DKLYRADSRP PDEIKRSGGL MPRGHNEYFD RGTQMNINLY
61: DHARGTQTGF VRYDDGYVST SLSLRSAHLA GQSILSGYST YYIYVIATAP NMFNVNDVLG
121: VYSPHPYEQE VSALGGIPYS QIYGWYRVNF GVIDERLHRN REYRDRYYRN LNIAPAEDGY
181: RLAGFPPDHQ AWREEPWIHH APQGCGNSSR TITGDTCNEE TQNLSTIYLR KYQSKVKRQI
241: FSDYQSEVDI YNRIRNEL