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Urease metallochaperone UreE, N-terminal domain superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   Urease metallochaperone UreE, N-terminal domain [ 69286]
Superfamily:   Urease metallochaperone UreE, N-terminal domain [ 69287]
Families:   Urease metallochaperone UreE, N-terminal domain [ 69288]

Superfamily statistics
Genomes (707) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 766 6,511 4
Proteins 766 6,511 4

Functional annotation
General category Processes_IC
Detailed category Protein modification

Function annotation of SCOP domain superfamilies

InterPro annotation
Cross references IPR004029 SSF69287 Protein matches

Urease and other nickel metalloenzymes are synthesised as precursors devoid of the metalloenzyme active site. These precursors then undergo a complex post-translational maturation process that requires a number of accessory proteins.

Members of this group are nickel-binding proteins required for urease metallocentre assembly [PubMed8318889]. They are believed to function as metallochaperones to deliver nickel to urease apoprotein [PubMed12072968, PubMed10753863]. It has been shown by yeast two-hybrid analysis that UreE forms a dimeric complex with UreG in Helicobacter pylori [PubMed12388207]. The UreDFG-apoenzyme complex has also been shown to exist [PubMed11157956, PubMed7721685] and is believed to be, with the addition of UreE, the assembly system for active urease [PubMed7721685]. The complexes, rather than the individual proteins, presumably bind to UreB via UreE/H recognition sites.

The structure of Klebsiella aerogenes UreE reveals a unique two-domain architecture.The N-terminal domain is structurally related to a heat shock protein, while the C-terminal domain shows homology to the Atx1 copper metallochaperone [PubMed11591723, PubMed11602602]. Significantly, the metal-binding sites in UreE and Atx1 are distinct in location and types of residues despite the relationship between these proteins and the mechanism for UreE activation of urease is proposed to be different from the thiol ligand exchange mechanism used by the copper metallochaperones.

The N-terminal domain is termed the peptide-binding domain. Deletion of this domain does not eliminate enzymatic activity, and the truncated protein can still activate urease [PubMed15866948].

InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.

Alignments of sequences to 3 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.

Browse and view proteins in genomes which have different domain combinations including a Urease metallochaperone UreE, N-terminal domain domain.

Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.

Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 3 hidden Markov models representing the Urease metallochaperone UreE, N-terminal domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]