{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Huanying Pang"],"species":["Vibrio Mimicus Vm603"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0003509000"],"submitter_email":["phying1218@163.com"],"submitter_affiliation":["Fisheries College of Guangdong Ocean University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["Protein lysine acetylation is an evolutionarily conserved post-translational modification (PTM), which is dynamic and reversible, playing a crucial regulatory role in almost every aspect of metabolism, of both eukaryotes and prokaryotes. Several global lysine acetylome studies have been carried out in various bacteria, but thus far, there have been no reports of lysine acetylation for the commercially important aquatic animal pathogen <i>Vibrio mimicus.</i> In the present study, we used anti-Ac-K antibody beads to highly sensitive immune-affinity purification and combined high-resolution LC-MS/MS to perform the first global lysine acetylome analysis in <i>V. mimicus</i>, leading to the identification of 1,097 lysine-acetylated sites on 582 proteins, and more than half (58.4%) of the acetylated proteins had only one site. The analysis of acetylated modified peptide motifs revealed six significantly enriched motifs, namely, KacL, KacR, L(-2) KacL, LKacK, L(-7) EKac, and IEKac. In addition, bioinformatic assessments state clearly that acetylated proteins have a hand in many important biological processes in <i>V. mimicus</i>, such as purine metabolism, ribosome, pyruvate metabolism, glycolysis/gluconeogenesis, the TCA cycle, and so on. Moreover, 13 acetylated proteins were related to the virulence of <i>V. mimicus</i>. To sum up, this is a comprehensive analysis whole situation protein lysine acetylome in <i>V. mimicus</i> and provides an important foundation for in-depth study of the biological function of lysine acetylation in <i>V. mimicus</i>."],"pubmed_title":["A Comprehensive Analysis of the Lysine Acetylome in the Aquatic Animals Pathogenic Bacterium <i>Vibrio mimicus</i>."],"pubmed_authors":["Wang Junlin J, Pang Huanying H, Yin Linlin L, Zeng Fuyuan F, Wang Na N, Hoare Rowena R, Monaghan Sean J SJ, Li Wanxin W, Jian Jichang J"],"additional_accession":[]},"is_claimable":false,"name":"The lysine acetylome in Vibrio mimicus","description":"In the present study, we performed the first global lysine acetylome in V. mimicus through a combination of highly sensitive immune-affinity purification and high-resolution LC−MS/MS, and identified 1097 lysine-acetylated sites on 582 proteins. Of the acetylated proteins, more than half were acetylated on one site. In the acetylome of V. mimicus, six significantly enriched motifs were identified and obtained including KacL, KacR, L(-2)KacL, LKacK, L(-7)EKac, and IEKac. In addition, bioinformatics results indicated that acetylated proteins participate in many different biological functions in V. mimicus, such as purine metabolism, ribosome, pyruvate metabolism, glycolysis / gluconeogenesis, TCA cycle, and so on. Moreover, 13 acetylated proteins were related to the virulence of V. mimicus.","dates":{"publication":"Tue Sep 14 00:00:00 GMT+01:00 2021"},"accession":"PXD028467","cross_references":{"TAXONOMY":["671074"],"pubmed":["35250932"]}}