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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
FunctionEssential for the cyclopropanation function. Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. Mycolic acids, which represent the major constituent of mycobacterial cell wall complex, act as substrates [catalytic activity: S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid].
ProductCyclopropane-fatty-acyl-phospholipid synthase 2 CmaA2 (cyclopropane fatty acid synthase) (CFA synthase) (cyclopropane mycolic acid synthase 2) (mycolic acid trans-cyclopropane synthetase)
CommentsRv0503c, (MTCY20G9.30c), len: 302 aa. CmaA2 (alternate gene name: cma2), cyclopropane-fatty-acyl-phospholipid synthase 2 (mycolic acid trans-cyclopropane synthetase) (see citations below). Note that this protein has 302 aa and not 322 aa: we have chosen a different initiation codon on the basis of homology. Equivalent to S72886|B2168_F3_130 hypothetical protein from Mycobacterium leprae (308 aa), FASTA score: (78.9% identity in 303 aa overlap); and highly similar to other proteins from Mycobacterium leprae. Also similar to other proteins from Mycobacterium tuberculosis and Mycobacterium bovis BCG e.g. MTV038_14|UMAA2|Rv0470c|MTV038.14 putative mycolic acid synthesis/modification protein (287 aa) (57.2% identity in 297 aa overlap).
Functional categoryLipid metabolism
ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in the culture filtrate and whole cell lysates of M. tuberculosis H37Rv but not the membrane protein fraction (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011).
MutantNon-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Disruption of this gene provides a growth advantage 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 and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Required for survival in primary murine macrophages, by transposon site hybridization (TraSH) in H37Rv (See Rengarajan et al., 2005). Non-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
CDS593871594779-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0503c|cmaA2
MTSQGDTTSGTQLKPPVEAVRSHYDKSNEFFKLWLDPSMTYSCAYFERPDMTLEEAQYAKRKLALDKLNLEPGMTLLDIGCGWGSTMRHAVAEYDVNVIGLTLSENQYAHDKAMFDEVDSPRRKEVRIQGWEEFDEPVDRIVSLGAFEHFADGAGDAGFERYDTFFKKFYNLTPDDGRMLLHTITIPDKEEAQELGLTSPMSLLRFIKFILTEIFPGGRLPRISQVDYYSSNAGWKVERYHRIGANYVPTLNAWADALQAHKDEAIALKGQETYDIYMHYLRGCSDLFRDKYTDVCQFTLVK
      
Bibliography