PXD013895

PXD013895 is an original dataset announced via ProteomeXchange.

Title	Systematic analysis of lysine acetylome reveals potential functions of lysine acetylation in Shewanellabaltica, the specific spoilage organism of aquatic products
Description	Protein lysine acetylation is a major post-translational modification and plays a critical regulatory role in almost every aspect in both eukaryotes and prokaryotes, yet there have been no data on Shewanellabaltica, which is one of the specific spoilage organism (SSO) of aquatic products.Here, we performed the first global acetylproteome analysis of S. baltica. 2929 lysine acetylation sites were identified in 1103 proteins, accounting for 26.1% of the total proteins which participate in a wide variety of biological processes, especially in the constituent of ribosome, the biosynthesis of aminoacyl-tRNA, the amino acids and fatty acid metabolism. Besides, 14 conserved acetylation motifs were detected in S. baltica. Notably, various directly or indirectly spoilage-related proteins were prevalently acetylated, including enzymesinvolved in the unsaturated fatty acids biosynthesis closely related to the cold adaptability,coldshock proteins,pivotal enzymesinvolved in the putrescinebiosynthesis,and a LuxR-type protein in quorum sensing system. The acetylome analysis in Shewanella can supplement the database and provide new insight into uncovering the spoilagemechanisms of S. baltica. The provided dataset illuminates the potential role of reversible acetylation in S. baltica, and serves as an important resource for exploring the physiological role of lysine acetylation in prokaryotes.
HostingRepository	PRIDE
AnnounceDate	2019-07-22
AnnouncementXML	Submission_2019-07-22_08:39:00.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Feifei Wang
SpeciesList	scientific name: Shewanella baltica; NCBI TaxID: 62322;
ModificationList	acetylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2019-05-17 03:48:40	ID requested
⏵ 1	2019-07-22 08:39:01	announced

Wang Y, Wang F, Bao X, Fu L, Systematic analysis of lysine acetylome reveals potential functions of lysine acetylation in Shewanella baltica, the specific spoilage organism of aquatic products. J Proteomics, 205():103419(2019) [pubmed]

submitter keyword: Lysine acetylation, Shewanella. baltica, metabolism, cold adaptability, quorum sensing

Linglin Fu
contact affiliation	Key Laboratory for Food Microbial Technology of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China
contact email	fulinglin@mail.zjgsu.edu.cn
lab head
Feifei Wang
contact affiliation	Key Laboratory for Food Microbial Technology of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou
contact email	291557843@qq.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/07/PXD013895

PRIDE project URI

• PRIDE
  1. PXD013895
     1. Label: PRIDE project
     2. Name: Systematic analysis of lysine acetylome reveals potential functions of lysine acetylation in Shewanellabaltica, the specific spoilage organism of aquatic products