Gene Rv0242c
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in the fatty acid biosynthesis pathway (first reduction step) [catalytic activity: (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = 3-oxoacyl-[acyl-carrier protein] + NADPH]. |
| Product | Probable 3-oxoacyl-[acyl-carrier protein] reductase FabG4 (3-ketoacyl-acyl carrier protein reductase) |
| Comments | Rv0242c, (MTV034.08c), len: 454 aa. Probable fabG4, 3-oxoacyl-[acyl-carrier protein] reductase, equivalent to 3063883|CAA18568.1|AL022486|MLCB1883_13|T44878 3-oxoacyl-[acyl-carrier protein] reductase homolog from Mycobacterium leprae (454 aa), FASTA scores: opt: 2486, E(): 0, (84.8% identity in 454 aa overlap). C-terminal part highly similar to many FabG proteins e.g. U39441|VHU3944 1_2 from Vibrio harveyi (244 aa), FASTA scores: opt: 562, E(): 3.4e-28, (40.2% identity in 241 aa overlap); U91631|PAU91631_3 from Pseudomonas aeruginosa (247 aa), FASTA scores: opt: 584, E(): 1.5e-29, (44.4% identity in 241 aa overlap). Has N-terminal extension of ~200 aa and C-terminal part contains PS00061 Short-chain dehydrogenases/reductases family signature. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| Functional category | Lipid metabolism |
| Proteomics | The product of this CDS corresponds to spots 1_266, 1_305 and 1_329 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (See Mollenkopf et al., 1999; Jungblut et al., 1999). Identified in carbonate extracts of M. tuberculosis H37Rv membranes using 2DGE and MALDI-MS (See Sinha et al., 2002). 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 in the cytosol and cell wall fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in both the aqueous and detergent phases of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-DGE, 2-DGE, and MALDI-TOF-MS (See Sinha et al., 2005). 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 M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh 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). |
| Transcriptomics | mRNA identified by microarray analysis and down-regulated after 24h of starvation (see Betts et al., 2002). |
| 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). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 290665 | 292029 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0242c|fabG4
VAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNLLAPLRLTEGLVGNGSIGEGGRVIGLSSIAGIAGNRGQTNYATTKAGMIGITQALAPGLAAKGITINAVAPGFIETQMTAAIPLATREVGRRLNSLLQGGQPVDVAEAIAYFASPASNAVTGNVIRVCGQAMIGA
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
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- Sinha S et al. [2002]. Proteome analysis of the plasma membrane of Mycobacterium tuberculosis. Proteomics
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- 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
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Sinha S, Kosalai K, Arora S, Namane A, Sharma P, Gaikwad AN, Brodin P and Cole ST [2005]. Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics. Proteomics
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Gurvitz A [2009]. The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2. Function Product
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. 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
- 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
