TABLE 3.
Cell wall-located proteins of B. subtilis 168a
| Protein | Function or similarity | Export signalb | SPase | Retention Signalc | Found in mediumd |
|---|---|---|---|---|---|
| Hag | Flagellin protein | − | − | − | Y |
| LytB | Modifier protein of autolysin LytC | Sec | SPase I | CWB | N |
| LytC | N-Acetylmuramoyl-l-alanine amidase | Sec | SPase I | CWB | N |
| WapA | Cell wall-associated protein precursor | RR | SPase I | CWB | Y |
| WprA | Cell wall-associated protein precursor | RR | SPase I | − | Y |
| YqgA | Similar to unknown proteins of B. subtilis | Sec | SPase I | − | N |
| YwsB | Similar to unknown proteins of B. subtilis | Sec | SPase I | − | N |
All listed cell wall-located proteins were identified by 2D PAGE and subsequent MALDI-TOF mass spectrometry and/or N-terminal amino acid sequencing as described by Antelmann et al. (6). Putative signal peptides, SPase I cleavage sites, and cell wall-binding domains were predicted as described by Tjalsma et al. (129). −, absence of known signal peptides, SPase I cleavage sites, or cell wall-binding proteins.
Identified transient export signals are Sec-type signal peptides (Sec) and RR-type signal peptides (RR).
Identified retention signals present in the mature part of the protein after processing by specific SPases are cell wall-binding domains (CWB).
The presence (Y) or absence (N) of a particular protein of the cell wall proteome in the growth medium is indicated.