TABLE 1.
Signal peptides used for Dac secretion in B. subtilis WB600
| Name | Amino acid sequencea | Charge in N regionb | Hydrophobic amino acidc |
|---|---|---|---|
| YncM | MAKPLSKGGILVKKVLIAGAVGTAVLFGTLSSGIPGLPAADAQVAKA | 4 | 35 |
| Bpr | MRKKTKNRLISSVLSTVVISSLLFPGAAGA | 3 | 17 |
| YwbN | MSDEQKKPEQIHRRDILKWGAMAGAAVA | 0 | 15 |
| AnsZ | MKKQRMLVLFTALLFVFTGCSHS | 2 | 13 |
| YvgO | MKRIRIPMTLALGAALTIAPLSFASA | 3 | 19 |
| AmyE | MFAKRFKTSLLPLFAGFLLLFHLVLAGPAAASA | 3 | 26 |
| OppA | MKKRWSIVTLMLIFTLVLSA | 3 | 13 |
| Vpr | MKKGIIRFLLVSFVLFFALSTGITGVQA | 2 | 20 |
| LipA | MKFVKRRIIALVTILMLSVTSLFALQPSAKA | 4 | 20 |
| WapA | MKKRKRRNFKRFIAAFLVLALMISLVPADVLA | 7 | 21 |
| Epr | MKNMSCKLVVSVTLFFSFLTIGPLAHA | 1 | 17 |
| YclQ | MKKFALLFIALVTAVVISACGNQSTSSKG | 2 | 17 |
a
Boldface letters present the hydrophobic H domain. The residues at positions −3 to −1 relative to the predicted signal peptidase (SPase) cleavage sites are underlined.
b
Calculated with aspartate and glutamate defined as −1, arginine and lysine defined as +1, and any other amino acid defined as 0.
c
Amino acids G, A, V, L, I, M, F, W, and P were defined as hydrophobic, and the other residues were characterized as hydrophilic.