Protein Family Models

HdeA (hns-dependent expression protein A) is a single domain alpha-helical protein localised in the periplasmic space. HdeA is involved in acid resistance essential for infectivity of enteric bacterial pathogens. Functional studies demonstrate that HdeA is activated by a dimer-to-monomer transition at acidic pH, leading to suppression of aggregation by acid-denatured proteins. The gene encoding HdeA was initially identified as part of an operon regulated by the nucleoid protein H-NS [1,2]. This family also contains HdeB [3]. [1]. 10623550. HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. Gajiwala KS, Burley SK;. J Mol Biol 2000;295:605-612. [2]. 9731767. Crystal structure of Escherichia coli HdeA. Yang F, Gustafson KR, Boyd MR, Wlodawer A;. Nat Struct Biol 1998;5:763-764. [3]. 17085547. Escherichia coli HdeB is an acid stress chaperone. Kern R, Malki A, Abdallah J, Tagourti J, Richarme G;. J Bacteriol. 2007;189:603-610. (from Pfam)

Date:

2024-10-16

Gene:

hdeB

Date:

2020-10-26

HdeB is a periplasmic, ATP-independent chaperone that is activated at very low pH (2-3) and has many protein substrates.

Gene:

hdeB

Date:

2019-03-06

HdeA family protein similar to acid-activated periplasmic chaperone HdeA, an acid-resistant chaperone that functions at low pH when it undergoes a transition from a well-folded dimer to an unfolded monomer, exposing hydrophobic surfaces that allows binding to a broad range of client proteins

Date:

2017-03-02