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. 2009 Jun 12;8(9):2170–2185. doi: 10.1074/mcp.M900088-MCP200

Table III. Qualitative analysis of glycoproteins from the periplasmic protein extracts of C. jejuni 11168 (wt) and the isogenic pglD mutant.

Accession number Gene name Protein name Precursora z Sequences of identified glycopeptidesb Oligosaccharide compositionc Ion scored Sequence coverage RT
m/z % min
YP_002343627 Cj0168c Putative periplasmic protein 940.14 3 (F)ANTPSDVNQTHTK(A) BacGalNAc5Glc 23 16.0
926.14 3 deAcBacGalNAc5Glc 79 15.2
NP_281430 Cj0235c Protein export membrane protein 1035.21 3 (N)SIAPSAPQLPSDVNSSK(−) BacGalNAc5Glc 14 24.8
1021.20 3 deAcBacGalNAc5Glc 55 23.6
YP_002343658 Cj0200c Putative periplasmic protein 962.14 3 (K)LEGTIAQIYDNNK (T) BacGalNAc5Glc 11 25.8
948.14 3 deAcBacGalNAc5Glc 97 24.2
CAL34323 Cj0152c Hypothetical protein 1231.31 3 (K)NISIENNISENNTTLLDEEK(N) BacGalNAc5Glc 6 27.2
1218.64 3 deAcBacGalNAc5Glc 66 27.0
YP_002345038 Cj1670c Putative membrane protein or CgpAe 1036.22 3 (K)TDQNITLVAPPEFQK(E) BacGalNAc5Glc 7 29.2
1022.22 3 deAcBacGalNAc5Glc 57 27.4
YP_002343574 Cj0864 Putative periplasmic protein 1058.10 3 (K)DoxiMNVSK(A) BacGalNAc5Glc 49 5 19.7
1037.10 3 deAcBacGalNAc5Glc
YP_002344271 Cj0114 Putative periplasmic protein 1133.05 4 (K)TITPSVVVSTTDSNSTIENNNTQNTQDDK(A) BacGalNAc5Glc 26 25.6
1122.55 4 deAcBacGalNAc5Glc 72 24.5
Putative periplasmic protein 1295.35 3 (R)LSQVEENNQNIENNFTSEIQK(L) BacGalNAc5Glc 60 27.5
1281.40 3 deAcBacGalNAc5Glc 25.6
YP_002344190 Cj0783 Periplasmic nitrate reductase cytochrome c-type subunit 1692.12 2 (K)VNLVEANFTTLQPGESTR(F) BacGalNAc5Glc 41 10 29.7
1671.12 2 deAcBacGalNAc5Glc

a The m/z and charge of precursors (MS2 fragments) for acquisition of MS3 spectra are provided in supplemental Fig. S2.

b The periplasmic protein, Cj0114, is identified by two peptides, and all other glycoproteins identified are single-peptide-based.

c Bac, 2,4-diacetamido-2,4,6-trideoxyglucopyronose; deAcBac, 2-acetamido-4-amino-2,4,6-trideoxyglucopyronose, i.e. deAcBac is monoacetylated Bac at the C-2 position only (30, 39, 40). The consensus sequence of possible N-glycosylation sites for prokaryotic proteins are highlighted (32). oxiM, oxidized methionine; wt, wild-type; ″, the same as above.

d Ion scores are available only for precursors on which MS3 were acquired and used for database searches with 0.00% false positive rate.

e According to Linton et al. (41).