Gene Rv2931
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Involved in phenolpthiocerol and phthiocerol dimycocerosate (dim) biosynthesis: extension of C18 with malony CoA (partial reduction). |
Product | Phenolpthiocerol synthesis type-I polyketide synthase PpsA |
Comments | Rv2931, (MTCY338.20), len: 1876 aa. PpsA, type-I polyketide synthase (see citations below), highly similar to others from Mycobacterium leprae e.g. Q9Z5K6|ML2357|MLCB12.02c putative polyketide synthase from Mycobacterium leprae (1871 aa), FASTA scores: opt: 7566, E(): 0, (76.1% identity in 1888 aa overlap); Q9S384|ML2356|MLCB12.01c putative polyketide synthase from Mycobacterium leprae (1540 aa), FASTA scores: opt: 4026, E(): 9.8e-212, (45.7% identity in 1811 aa overlap); Q49932|PKSC|L518_F1_2 putative polyketide synthase (1446 aa), FASTA scores: opt: 4026, E(): 9.4e-212, (70.6% identity in 885 aa overlap). Also similar to polyketide synthases from other bacteria e.g. C-terminus of Q9L8C7|EPOC polyketide synthase from Polyangium cellulosum (7257 aa), FASTA scores: opt: 2592, E(): 5.2e-133, (32.55% identity in 2245 aa overlap); P22367|MSAS_PENPA 6-methylsalicylic acid synthase from Penicillium patulum (Penicillium griseofulvum) (1774 aa), FASTA scores: opt: 2391, E(): 0, (34.2% identity in 1815 aa overlap); etc. And also highly similar to others from Mycobacterium tuberculosis e.g. Q10978|PPSB_MYCTU|RV2932 phenolpthiocerol synthesis polyketide synthase (1538 aa), FASTA scores: opt: 4227, E(): 0, (46.8% identity in 1810 aa overlap) (gap in middle); etc. Contains PS00606 Beta-ketoacyl synthases active site, and PS00012 Phosphopantetheine attachment site. Note that Rv2931|ppsA belongs to the transcriptional unit Rv2930|fadD26-Rv2939|papA5 (proven experimentally). |
Functional category | Lipid metabolism |
Proteomics | Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 and 90 days (See Kruh et al., 2010). 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). Translational start site supported by proteomics data (See Kelkar et al., 2011). |
Transcriptomics | mRNA identified by DNA microarray analysis: possibly down-regulated by hrcA|Rv2374c (see Stewart et al., 2002) and down-regulated after 24h of starvation (see Betts et al., 2002). DNA microarrays show lower 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). Non essential gene by Himar1 transposon mutagenesis in CDC1551 strain (see Lamichhane et al., 2003). 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 | 3245445 | 3251075 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2931|ppsA MTGSISGEADLRHWLIDYLVTNIGCTPDEVDPDLSLADLGVSSRDAVVLSGELSELLGRTVSPIDFWEHPTINALAAYLAAPEPSPDSDAAVKRGARNSLDEPIAVVGMGCRFPGGISCPEALWDFLCERRSSISQVPPQRWQPFEGGPPEVAAALARTTRWGSFLPDIDAFDAEFFEISPSEADKMDPQQRLLLEVAWEALEHAGIPPGTLRRSATGVFAGACLSEYGAMASADLSQVDGWSNSGGAMSIIANRLSYFLDLRGPSVAVDTACSSSLVAIHLACQSLRTQDCHLAIAAGVNLLLSPAVFRGFDQVGALSPTGQCRAFDATADGFVRGEGAGVVVLKRLTDAQRDGDRVLAVICGSAVNQDGRSNGLMAPNPAAQMAVLRAAYTNAGMQPSEVDYVEAHGTGTLLGDPIEARALGTVLGRGRPEDSPLLIGSVKTNLGHTEAAAGIAGFIKTVLAVQHGQIPPNQHFETANPHIPFTDLRMKVVDTQTEWPATGHPRRAGVSSFGFGGTNAHVVIEQGQEVRPAPGQGLSPAVSTLVVAGKTMQRVSATAGMLADWMEGPGADVALADVAHTLNHHRSRQPKFGTVVARDRTQAIAGLRALAAGQHAPGVVNPADGSPGPGTVFVYSGRGSQWAGMGRQLLADEPAFAAAVAELEPVFVEQAGFSLHDVLANGEELVGIEQIQLGLIGMQLALTELWCSYGVRPDLVIGHSMGEVAAAVVAGALTPAEGLRVTATRSRLMAPLSGQGGMALLELDAPTTEALIADFPQVTLGIYNSPRQTVIAGPTEQIDELIARVRAQNRFASRVNIEVAPHNPAMDALQPAMRSELADLTPRTPTIGIISTTYADLHTQPVFDAEHWATNMRNPVRFQQAIASAGSGADGAYHTFIEISAHPLLTQAIIDTLHSAQPGARYTSLGTLQRDTDDVVTFRTNLNKAHTIHPPHTPHPPEPHPPIPTTPWQHTRHWITTKYPAGSVGSAPRAGTLLGQHTTVATVSASPPSHLWQARLAPDAKPYQGGHRFHQVEVVPASVVLHTILSAATELGYSALSEVRFEQPIFADRPRLIQVVADNRAISLASSPAAGTPSDRWTRHVTAQLSSSPSDSASSLNEHHRANGQPPERAHRDLIPDLAELLAMRGIDGLPFSWTVASWTQHSSNLTVAIDLPEALPEGSTGPLLDAAVHLAALSDVADSRLYVPASIEQISLGDVVTGPRSSVTLNRTAHDDDGITVDVTVAAHGEVPSLSMRSLRYRALDFGLDVGRAQPPASTGPVEAYCDATNFVHTIDWQPQTVPDATHPGAEQVTHPGPVAIIGDDGAALCETLEGAGYQPAVMSDGVSQARYVVYVADSDPAGADETDVDFAVRICTEITGLVRTLAERDADKPAALWILTRGVHESVAPSALRQSFLWGLAGVIAAEHPELWGGLVDLAINDDLGEFGPALAELLAKPSKSILVRRDGVVLAPALAPVRGEPARKSLQCRPDAAYLITGGLGALGLLMADWLADRGAHRLVLTGRTPLPPRRDWQLDTLDTELRRRIDAIRALEMRGVTVEAVAADVGCREDVQALLAARDRDGAAPIRGIIHAAGITNDQLVTSMTGDAVRQVMWPKIGGSQVLHDAFPPGSVDFFYLTASAAGIFGIPGQGSYAAANSYLDALARARRQQGCHTMSLDWVAWRGLGLAADAQLVSEELARMGSRDITPSEAFTAWEFVDGYDVAQAVVVPMPAPAGADGSGANAYLLPARNWSVMAATEVRSELEQGLRRIIAAELRVPEKELDTDRPFAELGLNSLMAMAIRREAEQFVGIELSATMLFNHPTVKSLASYLAKRVAPHDVSQDNQISALSSSAGSVLDSLFDRIESAPPEAERSV
Bibliography
- Azad AK et al. [1997]. Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria. Homolog Mutant Function
- Cole ST et al. [1998]. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Sequence Secondary
- Camacho LR et al. [2001]. Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier. Mutant Function
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Regulation
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Walters SB et al. [2006]. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis. Transcriptome
- Chalut C et al. [2006]. The nonredundant roles of two 4'-phosphopantetheinyl transferases in vital processes of Mycobacteria. Biochemistry
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- 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