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. 2004 Jun;68(2):207–233. doi: 10.1128/MMBR.68.2.207-233.2004

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
a

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.

b

Identified transient export signals are Sec-type signal peptides (Sec) and RR-type signal peptides (RR).

c

Identified retention signals present in the mature part of the protein after processing by specific SPases are cell wall-binding domains (CWB).

d

The presence (Y) or absence (N) of a particular protein of the cell wall proteome in the growth medium is indicated.