Gene Rv0733
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | This small ubiquitous enzyme is essential in intracellular nucleotide metabolism, in addition it has been found to act as both a nucleoside mono- and DI-phosphate kinase suggesting it may have a role in RNA and DNA biosynthesis [catalytic activity: ATP + AMP = ADP + ADP]. |
| Product | Adenylate kinase Adk (ATP-AMP transphosphorylase) |
| Comments | Rv0733, (MTV041.07), len: 181 aa. adk, adenylate kinase (ATP-AMP transphosphorylase), equivalent to Z98756|MLCB24 92_28 probable adenylate kinase from Mycobacterium leprae (181 aa), FASTA scores: opt: 978, E(): 0, (83.6% identity in 177 aa overlap); and AAF86323.1|AF271342 putative adenylate kinase from Mycobacterium marinum (124 aa) (N-terminus shorter). Also highly similar to others e.g. P43414|KAD_STRCO adenylate kinase from Streptomyces coelicolor (217 aa), FASTA score: (43.0% identity in 186 aa overlap); etc. Contains PS00113 Adenylate kinase signature. Belongs to the adenylate kinase family. |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | The product of this CDS corresponds to spot 3_194 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and spot 0733 identified in short term culture filtrate by proteomics at the Statens Serum Institute (Denmark) (see citations below). Identified in immunodominant fractions of M. tuberculosis H37Rv cytosol using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). |
| Mutant | Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 826122 | 826667 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0733|adk
VRVLLLGPPGAGKGTQAVKLAEKLGIPQISTGELFRRNIEEGTKLGVEAKRYLDAGDLVPSDLTNELVDDRLNNPDAANGFILDGYPRSVEQAKALHEMLERRGTDIDAVLEFRVSEEVLLERLKGRGRADDTDDVILNRMKVYRDETAPLLEYYRDQLKTVDAVGTMDEVFARALRALGK
Bibliography
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Meena LS, Chopra P, Bedwal RS and Singh Y [2003]. Nucleoside diphosphate kinase-like activity in adenylate kinase of Mycobacterium tuberculosis. Product Biochemistry Function
- Miron S et al. [2004]. Structural and dynamic studies on ligand-free adenylate kinase from Mycobacterium tuberculosis revealed a closed conformation that can be related to the reduced catalytic activity. Structure
- Bellinzoni M, Haouz A, Grana M, Munier-Lehmann H, Shepard W and Alzari PM [2006]. The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer. Structure
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
