Protein Family Models

HypA is a metallochaperone that binds nickel to bring it safely to its target. The targets for Hypa are the nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. The nickel coordinates with four nitrogens within the protein. The four conserved cysteines towards the C-terminus bind one zinc moiety probably to stabilise the protein fold [1]. [1]. 19621959. Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites. Xia W, Li H, Sze KH, Sun H;. J Am Chem Soc. 2009;131:10031-10040. (from Pfam)

Date:

2024-10-16

hydrogenase maturation nickel metallochaperone HypA is required for nickel insertion into the metal center of the hydrogenase

Date:

2018-03-07

Plays a role in hydrogenase/urease nickel cofactor insertion

Date:

2020-10-26

Plays a role in hydrogenase/urease nickel cofactor insertion

Gene:

hypA

Date:

2020-10-26

CXXC-~12X-CXXC and genetically seems a regulatory protein. In Hpylori, hypA mutant abolished hydrogenase activity and decrease in urease activity. Nickel supplementation in media restored urease activity and partial hydrogenase activity. HypA probably involved in inserting Ni in enzymes.

Gene:

hypA

Date:

2024-06-14