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. 2021 Nov 19;203(24):e00393-21. doi: 10.1128/JB.00393-21

TABLE 1.

Envelope proteins that copurified with LbcA and were also isolated by an LbcA-CtpA-S302A protease trapa

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
a

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).

b

Rank based on the average number of peptide spectral matches among 67 cell envelope proteins that copurified with LbcA-FLAG (Table S6).

c

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).

d

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.