Gene Rv1180
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Potentially involved in some intermediate steps for the synthesis of a polyketide molecule which may be involved in secondary metabolism. Supposedly involved in stationary-phase survival. |
| Product | Probable polyketide beta-ketoacyl synthase Pks3 |
| Comments | Rv1180, (MTV005.16), len: 488 aa. Probable polyketide beta-ketoacyl synthase, equivalent to a predicted homologous protein from Mycobacterium smegmatis (see citation below), and similar to the N-terminus of many polyketide synthases e.g. MCAS_MYCBO|Q02251 mycocerosic acid synthase from Mycobacterium bovis (2110 aa), FASTA scores: opt: 2115, E(): 0, (66.5% identity in 472 aa overlap). Also similar to, and same length as P96284|Z83858|MTCY24G1.02 M. tuberculosis (496 aa), FASTA scores: opt: 1424, E(): 0, (50.9% identity in 444 aa overlap). Contains possible signal sequence and PS00013 Prokaryotic membrane lipoprotein lipid attachment site, also PS00606 Beta-ketoacyl synthases active site. Belongs to the beta-ketoacyl-ACP synthases family. Alternative nucleotide at position 1315191 (a->C; Stop489Y) has been observed. Rv1180/Rv1181 fusion has been called msl3. |
| Functional category | Lipid metabolism |
| Proteomics | Identified by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011). |
| Transcriptomics | DNA microarrays and qRT-PCR show higher level of expression in M. tuberculosis H37Rv than in phoP|Rv0757 mutant (See Walters et al., 2006). |
| 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). M. tuberculosis H37Rv msl3|Rv1180/Rv1181 mutant aggregates in liquid culture and does not produce mycolipanoic, mycolipenic, or mycolipodienoic acids (See Dubey et al., 2002). 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
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 1313725 | 1315191 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1180|pks3
VRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLG
Bibliography
- Keer J, Smeulders MJ, Gray KM and Williams HD [2000]. Mutants of Mycobacterium smegmatis impaired in stationary-phase survival. Homolog Mutant Function
- Dubey VS et al. [2002]. Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation. Mutant Sequence
- Walters SB et al. [2006]. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis. Transcriptome
- 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
