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. 2002 May;70(5):2271–2277. doi: 10.1128/IAI.70.5.2271-2277.2002

FIG. 1.

FIG. 1.

Alignment of CesF amino acid sequence from EHEC O157:H7 (O157) with the 120-amino-acid CesF sequence of EPEC E2348/69 (O127:H6) and the 119-amino-acid CesF sequence of RDEC1. The region of similarity of the chaperone FanE with CesF is also shown. Identical amino acids are indicated by periods, similar amino acids are indicated by plus signs, and dissimilar amino acids are indicated by spaces. The percentages of identity (%id) and similarity (siml) relative to the O157:H7 sequence are indicated at the ends of the aligned sequences. Structural details (struct.) were predicted by Jpred and are indicated above the CesF amino acid sequence as follows: a, α-helix; b, β sheet; boldface type, potential amphipathic regions. Also indicated in the CesF amino acid sequence are paired cysteine residues (underlined) and the large number of L, I, and V residues (boldface type) that occur, especially in the α-helices.