PXD052460

PXD052460 is an original dataset announced via ProteomeXchange.

Dataset Summary

Title	A new target of multiple lysine methylation in bacteria
Description	The methylation of ε-amino groups in protein lysine residues is an important posttranslational modification in eukaryotes, influencing various biological processes. In prokaryotes, this modification has been less studied, but recent findings suggest its role in bacterial immune evasion and host cell adhesion. Here, we analyzed Acinetobacter sp. Tol 5 cell surface proteins using LC‒MS, discovering that lysine residues of its trimeric autotransporter adhesin (TAA), AtaA, are specifically methylated. Over 130 of 232 lysine residues in AtaA were methylated. We identified the outer membrane protein lysine methyltransferase (OM PKMT) KmtA, responsible for the methylation. Bioinformatic analysis revealed the wide distribution of OM PKMT genes among gram-negative bacteria, including pathogens with TAAs that promote infection, such as Burkholderia mallei and Haemophilus influenzae. Clustering analysis suggested that KmtA is a new type of OM PKMT. Deletion of Tol 5 KmtA increased AtaA on the cell surface, enhancing adhesion and slowing growth.
HostingRepository	jPOST
AnnounceDate	2024-05-22
AnnouncementXML	Submission_2024-05-21_22:38:18.474.xml
DigitalObjectIdentifier
ReviewLevel	Non peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Shori Inoue
SpeciesList	scientific name: Acinetobacter sp. Tol 5; NCBI TaxID: 710648;
ModificationList	L-methionine sulfoxide; alpha-amino acetylated residue; N6,N6-dimethyl-L-lysine; monomethylated L-lysine; N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue); S-carboxamidomethyl-L-cysteine
Instrument	Q Exactive

Dataset History

Revision	Datetime	Status	ChangeLog Entry
0	2024-05-21 22:38:15	ID requested
⏵ 1	2024-05-21 22:38:18	announced

Publication List

Dataset with its publication pending

Dataset with its publication pending

Keyword List

submitter keyword: posttranslational modification, protein lysine methylation, trimeric autotransporter adhesin, bacterial adhesion

submitter keyword: posttranslational modification, protein lysine methylation, trimeric autotransporter adhesin, bacterial adhesion

Contact List

Katsutoshi Hori
lab head
Shori Inoue
contact affiliation	Nagoya University
dataset submitter

Full Dataset Link List

jPOST dataset URI
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jPOST dataset URI

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.jpostdb.org/JPST003124/