Gene Rv3628
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in the function of cellular bioenergetics [catalytic activity: pyrophosphate + H(2)O = 2 orthophosphate]. |
| Product | Inorganic pyrophosphatase Ppa (pyrophosphate phospho-hydrolase) (PPASE) (inorganic diphosphatase) (diphosphate phospho-hydrolase) |
| Comments | Rv3628, (MTCY15C10.24), len: 162 aa. Ppa, inorganic pyrophosphatase (see Triccas & Gicquel 2001), identical to O69540|IPYR_MYCLEPPA|ML0210|MLCB2548.21 inorganic pyrophosphatase from Mycobacterium leprae (162 aa) FASTA scores: opt: 1018, E(): 1.3e-59, (89.5% identity in 162 aa overlap). Also highly similar to many bacterial pyrophosphatases e.g. Q9X8I9|IPYR_STRCO|PPA|SCE9.16 from Streptomyces coelicolor (163 aa), FASTA scores: opt: 773, E(): 1.3e-43, (67.5% identity in 163 aa overlap); O05545|IPYR_GLUOX|PPA from Gluconobacter oxydans (Gluconobacter suboxydans) (176 aa), FASTA scores: opt: 553, E(): 3.2e-29, (53.8% identity in 145 aa overlap); P77992|IPYR_THELI|PPA from Thermococcus litoralis (176 aa) FASTA scores: opt: 537, E(): 3.5e-28, (49.35% identity in 152 aa overlap); P50308|IPYR_SULAC|PPA from Sulfolobus acidocaldarius (173 aa), FASTA scores: opt: 518, E(): 6e-27, (45.3% identity in 159 aa overlap); etc. Belongs to the PPASE family. Cofactor: requires the presence of divalent metal cation. Magnesium confers the highest activity. Binds 4 divalent cations per subunit (by similarity). |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | The product of this CDS corresponds to spot 3_138 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations). 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 and Edman degradation (See Mattow et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011). |
| Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 4067423 | 4067911 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3628|ppa
VQFDVTIEIPKGQRNKYEVDHETGRVRLDRYLYTPMAYPTDYGFIEDTLGDDGDPLDALVLLPQPVFPGVLVAARPVGMFRMVDEHGGDDKVLCVPAGDPRWDHVQDIGDVPAFELDAIKHFFVHYKDLEPGKFVKAADWVDRAEAEAEVQRSVERFKAGTH
Bibliography
- 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
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Triccas JA et al. [2001]. Analysis of stress- and host cell-induced expression of the Mycobacterium tuberculosis inorganic pyrophosphatase. Regulation
- Dahl JL et al. [2003]. The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Regulon
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. 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
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- 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
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
