Gene Rv1932 (cfp20)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Has antioxidant activity. Could remove peroxides or H(2)O(2) |
| Product | Probable thiol peroxidase Tpx |
| Comments | Rv1932, (MTCY09F9.32c), len: 165 aa. Probable tpx (alternate gene name: cfp20), thiol peroxidase similar to TPX_ECOLI|P37901 thiol peroxidase (p20) from Escherichia coli (167 aa), fasta scores: opt: 535, E(): 7.3e-25, (52.4% identity in 164 aa overlap). There are four other related enzymes in M. tuberculosis: Rv2428, Rv2521, Rv2238c, Rv1608c. |
| Functional category | Virulence, detoxification, adaptation |
| Proteomics | The product of this CDS corresponds to spot 3_32 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and also spots 1932 identified in short term culture filtrate and cell wall by the Statens Serum Institute (Denmark) (see citations below). Identified in immunodominant fractions of both M. tuberculosis H37Rv culture filtrate and cytosol using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). 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). Translational start site supported by proteomics data (See Kelkar et al., 2011). |
| Mutant | Non-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis H37Rv tpx|Rv1932 mutant shows increased sensitivity to oxidative and nitrosative stress in vitro; mutant shows growth defect in lungs and spleen of BALB/c mice; SCID mice infected with mutant live longer than those infected with wild-type; mutant shows growth defect in resting and activated bone marrow-derived macrophages from BALB/c, C57BL/6 and C57BL/6 iNOS-/- mice (See Hu and Coates 2009). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 2183372 | 2183869 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1932|tpx
MAQITLRGNAINTVGELPAVGSPAPAFTLTGGDLGVISSDQFRGKSVLLNIFPSVDTPVCATSVRTFDERAAASGATVLCVSKDLPFAQKRFCGAEGTENVMPASAFRDSFGEDYGVTIADGPMAGLLARAIVVIGADGNVAYTELVPEIAQEPNYEAALAALGA
Bibliography
- Weldingh K, Rosenkrands I, Jacobsen S, Rasmussen PB, Elhay MJ and Andersen P [1998]. Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins. 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
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. 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
- 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
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Rho BS et al. [2006]. Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis. Structure
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Hu Y et al. [2009]. Acute and persistent Mycobacterium tuberculosis infections depend on the thiol peroxidase TpX. Mutant
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- 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
