Table 2.
Functional annotation enrichment for 51 acetylated proteins with cobB-sensitive acetyllysine sites
| Term1 | Count2 | %3 | Fold enrichment4 | P-value4 | Bonferroni |
|---|---|---|---|---|---|
| Protein biosynthesis | 15 | 25.9 | 77.2 | 8.4E-23 | 9.9E-21 |
| Ribosome | 10 | 17.2 | 146.2 | 1.9E-17 | 2.3E-15 |
| Ribonucleoprotein | 10 | 17.2 | 107.7 | 3.5E-16 | 3.9E-14 |
| Ribosomal protein | 10 | 17.2 | 102.3 | 5.7E-16 | 6.6E-14 |
| Acetylation | 12 | 20.7 | 46.6 | 1.6E-15 | 1.8E-13 |
| RNA-binding | 7 | 12.1 | 30.8 | 1.0E-07 | 1.2E-05 |
| DNA binding | 7 | 12.1 | 27.7 | 1.9E-07 | 2.3E-05 |
| Phosphoprotein | 8 | 13.8 | 18.5 | 2.4E-07 | 2.8E-05 |
| Cytoplasm | 13 | 22.4 | 6.0 | 9.9E-07 | 1.2E-04 |
| DNA condensation | 4 | 6.9 | 192.6 | 1.1E-06 | 1.3E-04 |
| rRNA-binding | 4 | 6.9 | 64.2 | 3.3E-05 | 0.004 |
| Activator | 5 | 8.6 | 17.3 | 1.9E-04 | 0.022 |
| DNA binding | 11 | 19.0 | 4.1 | 2.6E-04 | 0.030 |
| Elongation factor | 3 | 5.2 | 74.4 | 7.3E-04 | 0.083 |
| Glycolysis | 3 | 5.2 | 43.9 | 0.002 | 0.219 |
| Methylated amino end | 2 | 3.4 | 327.5 | 0.006 | 0.508 |
| Transcription | 8 | 13.8 | 3.5 | 0.007 | 0.553 |
| Initiation factor | 2 | 3.4 | 272.9 | 0.007 | 0.573 |
| Duplication | 2 | 3.4 | 272.9 | 0.007 | 0.573 |
| Methylation | 3 | 5.2 | 23.0 | 0.007 | 0.584 |
| Methylated amino acid | 2 | 3.4 | 204.7 | 0.010 | 0.678 |
| Capsule biogenesis/degradation | 2 | 3.4 | 181.9 | 0.011 | 0.721 |
| Molecular chaperone | 2 | 3.4 | 136.5 | 0.014 | 0.817 |
| Heterodimer | 2 | 3.4 | 102.3 | 0.019 | 0.896 |
| Transcription regulation | 7 | 12.1 | 3.1 | 0.024 | 0.941 |
| Pyridoxal phosphate | 3 | 5.2 | 10.5 | 0.032 | 0.980 |
| Metal binding | 6 | 10.3 | 3.2 | 0.039 | 0.991 |
| Chaperone | 3 | 5.2 | 9.3 | 0.040 | 0.992 |
| Oxidoreductase | 6 | 10.3 | 3.1 | 0.042 | 0.994 |
1
SP_Pir keyword/GO ontology term.
2
Number of DAVID ID's matching the specific GOTERM.
3
% of count matching a specific GO category over total number of DAVID ID's entered for analysis (58).
4
Because our peptide-based affinity enrichment strategy achieved a dynamic range of about 7 orders of magnitude, identifying acetylated lysines from proteins with very low, as well as very high, estimated protein copy numbers per cell (Kuhn et al. 2014), we used the the E. coli proteome as background.