UreC is the cytoplasmic alpha and catalytic subunit of the three-chain bacterial urease. Within the UreABC complex it supplies the carbamylated lysine and ligands of the dinickel active site that hydrolyzes urea to ammonia and carbon dioxide after UreDEFG-dependent maturation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: UreC is a cytoplasmic subunit of soluble bacterial urease. Reason: The reviewed UniProt localization is coherent with the UreABC complex. |
| GO:0009039 urease activity | IEA GO_REF:0000120 | ACCEPT | Summary: UreC is the catalytic subunit that contains the complete dinickel urease active site. Reason: Requiring assembly with UreA and UreB does not make UreC a noncatalytic subunit. Structural evidence places the complete catalytic center in the UreC-equivalent alpha chain (PMID:8718850). |
| GO:0016151 nickel cation binding | IEA GO_REF:0000120 | ACCEPT | Summary: UreC contains the urease dinickel catalytic center. Reason: The alpha-subunit binickel site is directly established structurally (PMID:8718850). |
| GO:0016787 hydrolase activity | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: This is a broad parent of the supported urease activity. Reason: The ancestor is biologically true, but GO:0009039 is the informative reaction-specific function. |
| GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: This carbon-nitrogen hydrolase parent is compatible but less precise than urease activity. Reason: This ancestor is biologically true, while GO:0009039 captures the exact EC 3.5.1.5 reaction. |
| GO:0043419 urea catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: UreC provides the active site for the urea-catabolic reaction. Reason: Mature urease directly hydrolyzes urea. |
| GO:0035550 urease complex | IEA file:PSEPK/ureC/ureC-uniprot.txt | NEW | Summary: UreC is the catalytic alpha subunit of the UreABC urease complex. Reason: Reviewed UniProt and alpha-beta-gamma structural evidence support explicit complex membership. |
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Download this section (compressed HTML)Q: Is Q88J04 active-site occupancy and carbamylation nickel-limited in KT2440?
Experiment: Purify KT2440 UreABC and quantify UreC nickel occupancy, lysine carbamylation, and urea-hydrolysis kinetics before and after UreDEFG activation.
Hypothesis: UreDEFG increases Q88J04 lysine carbamylation and dinickel occupancy to generate active UreABC.
Type: Native complex purification, metal analysis, mass spectrometry, and enzyme kinetics
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