| General information | | DisProt: | DP00367 | | Name: | Urease accessory protein UreG | | Synonym(s): | UREG_BACPA
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q9RP19 | | UniGene: | | | SwissProt: | UREG_BACPA | | TrEMBL: | | | NCBI (GI): | 75420971 | | Source organism: | Bacillus pasteurii | | Sequence length: | 211 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKTIHLGIGG PVGSGKTTLV KTLSEALKEE YSIAVITNDI YTREDANFLI NENILEKDRI - 60
IGVETGGCPH TAIREDASMN FEAIEELKNR FDDLEIILLE SGGDNLSATF SPELVDAFIY - 120
VIDVSEGGDI PRKGGPGVTR SDFLMVNKTE LAPYVGVDLD TMKNDTIKAR NGRPFTFANI - 180
KTKKGLDEII AWIKSDLLLE GKTNESASES K
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| Functional narrative |
Urease is a nickel-containing enzyme found in plants, fungi, and bacteria that catalyzes the hydrolysis of urea in the last step of nitrogen mineralization. Bacillus pasteurii UreG is a chaperone involved in the urease active site assembly. Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by ureG. Exists in a relatively unstructured form; binding to the other subunits (ureD, ureF and apourease) may induce correct protein folding. The presence of Zn2+ or GTP does not alter the unfolded state.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 211 | | Length: | 211 | | Region sequence: |
MKTIHLGIGGPVGSGKTTLVKTLSEALKEEYSIAVITNDIYTREDANFLINENILEKDRI
IGVETGGCPHTAIREDASMNFEAIEELKNRFDDLEIILLESGGDNLSATFSPELVDAFIY
VIDVSEGGDIPRKGGPGVTRSDFLMVNKTELAPYVGVDLDTMKNDTIKARNGRPFTFANI
KTKKGLDEIIAWIKSDLLLEGKTNESASESK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Chaperones
| | Functional subclasses: | Cofactor/heme binding
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 8; 15N-enriched UreG; 5-mm reverse detection probe on a 1-mM sample; 800.13 MHz)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.5; 0.01-cm path length; 20 mM phosphate, 0.15 M NaCl)
- Size exclusion/gel filtration chromatography (298 K; pH: 8; 2.5 mg/ml protein; 50 mM Tris-HCl, 0.15 M NaCl; Superdex-75 HR 10/30 FPLC column)
| References:
- Zambelli B, Stola M, Musiani F, De Vriendt K, Samyn B, Devreese B, Van Beeumen J, Turano P, Dikiy A, Bryant DA, Ciurli S. "UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+." 2005; 280(6): 4684-95. PubMed: 15542602
| Comments:
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| References |
- Neyroz P, Zambelli B, Ciurli S. "Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and time-resolved fluorescence spectroscopy." Biochemistry. 2006; 45(29): 8918-30. PubMed: 16846235
- Zambelli B, Stola M, Musiani F, De Vriendt K, Samyn B, Devreese B, Van Beeumen J, Turano P, Dikiy A, Bryant DA, Ciurli S. "UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+." 2005; 280(6): 4684-95. PubMed: 15542602
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