Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Mar 31;12:643951. doi: 10.3389/fmicb.2021.643951

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2021 Qu, Zhao, Sun, Wu and Tao.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Conservation of phosphoacceptors in RmlA orthologs. (A) Multiple sequence alignment of RmlA sequences from Pseudomonas aeruginosa to mycobacterial species. The alignment was performed using ClustalW and Espript. Residues conserved in all species are shown in black boxes. The three phosphorylation sites of RmlA are indicated. Protein secondary element assignments are represented above the sequences. Numbering of amino acids corresponds to the RmlA protein from P. aeruginosa. (B) Localization of T12, T54, T197 phospho-sites in the three-dimensional structure of RmlA. Overall view (left panel) showing the RmlA monomer structure in ribbon representation with the α-helix and the β-sheet. Close-up view (right panel) indicates side chains of residues delineating the active site hydrophobic tunnel.