Protein Family Models

The structure of this domain is known and is similar to the periplasmic binding proteins [1]. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 9309218. The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement. Tyrrell R, Verschueren KH, Dodson EJ, Murshudov GN, Addy C, Wilkinson AJ;. Structure 1997;5:1017-1032. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

LrhA, as found in Escherichia coli and Salmonella enterica, is a LysR family pleiotropic regulator of genes involved in flagella synthesis, motility and chemotaxis. In some species, members of this family characterized for their regulation of systems such as type VI secretion (T6SS) may have more specific names, as with RovM (regulator of virulence M) in Yersinia.

Gene:

lrhA

Date:

2022-03-28

LysR family transcriptional regulator LrhA is involved in control of the transcription of flagellar, motility, and chemotaxis genes

Date:

2017-02-03