Reviewed,
UniProtKB/Swiss-Prot P0A664 (UREG_MYCTU)
Last modified
November 3, 2009.
Version 25.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Urease accessory protein ureG | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 224 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by ureG By similarity. |
| Subunit structure | Homodimer; disulfide-linked Probable. The physiological role of the disulfide bond has not been proven in vivo. UreD, ureF and ureG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of ureC. The ureE protein probably delivers the nickel By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the ureG family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nickel insertion |
| Cellular component | Cytoplasm |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Chaperone |
| PTM | Disulfide bond |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro GTP bindingInferred from electronic annotation. Source: UniProtKB-KW nickel ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 224 | 224 | Urease accessory protein ureG HAMAP MF_01389 | PRO_0000067669 | |||||
Regions | |||||||||
| Nucleotide binding | 32 – 39 | 8 | GTP By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 90 | Interchain Potential | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Purification, characterization, and genetic analysis of Mycobacterium tuberculosis urease, a potentially critical determinant of host-pathogen interaction." Clemens D.L., Lee B.-Y., Horwitz M.A. J. Bacteriol. 177:5644-5652(1995) [PubMed: 7559354] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35801 / TMC 107 / Erdman. |
| [2] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [3] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
| [4] | "Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family." Zambelli B., Musiani F., Savini M., Tucker P., Ciurli S. Biochemistry 46:3171-3182(2007) [PubMed: 17309280] [Abstract] Cited for: PROTEIN SEQUENCE OF 171-186 AND 193-224, SUBUNIT, GTPASE ACTIVITY, POSSIBLE DISULFIDE BOND, MODELING. |
Cross-references
Sequence databases | |
|---|---|
| U33011 Genomic DNA. Translation: AAC43477.1. BX842578 Genomic DNA. Translation: CAB06135.1. AE000516 Genomic DNA. Translation: AAK46171.1. | |
| PIR | D70665. |
| RefSeq | NP_216368.1. NP_336357.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 885729. 923708. |
| GenomeReviews | Gene locus MT1900 in contig AE000516_GR. Gene locus Rv1852 in contig AL123456_GR. |
| KEGG | mtc:MT1900. mtu:Rv1852. |
| TIGR | MT1900. |
Organism-specific databases | |
| TubercuList | Rv1852. |
Phylogenomic databases | |
| HOGENOM | P0A664. |
| OMA | VQIFVID. |
Family and domain databases | |
| HAMAP | MF_01389. [Tree] |
| InterPro | IPR003495. Cbl_biosynth_CobW-like. IPR012202. NiFe_hyd/urase_mat_GTPase. IPR004400. UreG. [Graphical view] |
| Pfam | PF02492. cobW. 1 hit. [Graphical view] |
| PIRSF | PIRSF005624. Ni-bind_GTPase. 1 hit. |
| TIGRFAMs | TIGR00101. ureG. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | UREG_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P0A664 Secondary accession number(s): P50051 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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