TABLE 1.
Protein | Predicted feature or function | Abundance rank with LbcAb | Abundance rank with LbcA-CtpA trapc | CtpA substrate of Srivastava et al.d |
---|---|---|---|---|
PA1198 | Peptidoglycan NlpC/P60 endopeptidase | 3 | 2 | Yes |
PA1048 | Peptidoglycan-binding OmpA C-terminal domain | 4 | 7 | NT |
RlpA | Peptidoglycan lytic transglycosylase | 5 | 4 | No |
MltD | Peptidoglycan lytic transglycosylase | 10 | 3 | No |
MltB1 | Peptidoglycan lytic transglycosylase | 13 | 6 | NT |
MepM | Peptidoglycan LytM/M23 endopeptidase | 18 | 1 | Yes |
AmiB | Peptidoglycan amidase | 65 | 23 | NT |
Cell envelope proteins that copurified with LbcA-CtpA-S302A, but not with LbcA-CtpA, following in vivo cross-linking (17) and also copurified with LbcA-FLAG from a ctpA-S302A strain in this study with average peptide spectral matches ≥5-fold higher than those in an LbcA no-FLAG-tag negative-control purification (see Tables S4 to S6 in the supplemental material).
Rank based on the average number of peptide spectral matches among 67 cell envelope proteins that copurified with LbcA-FLAG (Table S6).
Rank based on the average number of peptide spectral matches among 25 cell envelope proteins that copurified exclusively with the LbcA-CtpA-S302A trap (17).
In the study by Srivastava et al., a protein was classified as a CtpA substrate if a FLAG-tagged version accumulated in a ΔctpA mutant in vivo and the protein was degraded by CtpA in vitro (17). NT, not tested by Srivastava et al.