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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionInvolved in the function of cellular bioenergetics [catalytic activity: pyrophosphate + H(2)O = 2 orthophosphate].
ProductInorganic pyrophosphatase Ppa (pyrophosphate phospho-hydrolase) (PPASE) (inorganic diphosphatase) (diphosphate phospho-hydrolase)
CommentsRv3628, (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 categoryIntermediary metabolism and respiration
ProteomicsThe 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).
MutantEssential 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
TypeStartEndOrientation
CDS40674234067911+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3628|ppa
VQFDVTIEIPKGQRNKYEVDHETGRVRLDRYLYTPMAYPTDYGFIEDTLGDDGDPLDALVLLPQPVFPGVLVAARPVGMFRMVDEHGGDDKVLCVPAGDPRWDHVQDIGDVPAFELDAIKHFFVHYKDLEPGKFVKAADWVDRAEAEAEVQRSVERFKAGTH
      
Bibliography