Taxonomic distribution of proteins containing UreE_C domains

The UreE_C domain within your query sequence starts at position 121 and ends at position 282, and its E-value is 5.86e-35.

Crystal structure of Klebsiella aerogenes UreE, a nickel-bindingmetallochaperone for urease activation.

Song HK, Mulrooney SB, Huber R, Hausinger RP
J Biol Chem. 2001; 276: 49359-64

UreE is proposed to be a metallochaperone that delivers nickel ions tourease during activation of this bacterial virulence factor. Wild-typeKlebsiella aerogenes UreE binds approximately six nickel ions perhomodimer, whereas H144*UreE (a functional C-terminal truncated variant)was previously reported to bind two. We determined the structure ofH144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5A resolution. The present structure reveals an Hsp40-like peptide-bindingdomain, an Atx1-like metal-binding domain, and a flexible C terminus.Three metal-binding sites per dimer, defined by structural analysis ofCu-H144*UreE, are on the opposite face of the Atx1-like domain thanobserved in the copper metallochaperone. One metal bridges the twosubunits via the pair of His-96 residues, whereas the other two sitesinvolve metal coordination by His-110 and His-112 within each subunit. Incontrast to the copper metallochaperone mechanism involving thiol ligandexchanges between structurally similar chaperones and target proteins, wepropose that the Hsp40-like module interacts with urease apoprotein and/orother urease accessory proteins, while the Atx1-like domain delivershistidyl-bound nickel to the urease active site.