Gene Rv2932
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Involved in phenolpthiocerol and phthiocerol dimycocerosate (dim) biosynthesis: extension with malony CoA (partial reduction). |
Product | Phenolpthiocerol synthesis type-I polyketide synthase PpsB |
Comments | Rv2932, (MTV011.01, MTCY338.21, MT3002), len: 1538 aa. PpsB, type-I polyketide synthase (see citations below), highly similar to others from Mycobacterium leprae e.g. Q9S384|ML2356|MLCB12.01c putative polyketide synthase (1540 aa), FASTA scores: opt: 7284, E(): 0, (76.3% identity in 1561 aa overlap); Q49932|PKSC|L518_F1_2 putative polyketide synthase (1446 aa), FASTA scores: opt: 6811, E(): 0, (76.2% identity in 1462 aa overlap); etc. Also similar to polyketide synthases from other bacteria e.g. Q9KIZ6|EPOE EPOE protein from Polyangium cellulosum (3798 aa), FASTA scores: opt: 3052, E(): 3.3e-165, (38.35% identity in 1538 aa overlap); etc. And also highly similar to others from Mycobacterium tuberculosis e.g. Q10977|PPSA_MYCTU|RV2931 phenolpthiocerol synthesis polyketide synthase (1876 aa), FASTA scores: opt: 4227, E(): 0, (46.9% identity in 1810 aa overlap); P96203|PPSD|Rv2934|MTCY19H9.02 PKSE protein (1827 aa), FASTA scores: opt: 3756, E(): 1.8e-205, (42.9% identity in 1808 aa overlap); etc. Overlaps and extends CDS from neighbouring cosmid MTCY338.21. Contains PS00606 Beta-ketoacyl synthases active site. Note that Rv2932|ppsB belongs to the transcriptional unit Rv2930|fadD26-Rv2939|papA5 (proven experimentally). Nucleotide position 3254365 in the genome sequence has been corrected, T:C resulting in L1098L. |
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). |
Transcriptomics | 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). 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 | 3251072 | 3255688 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2932|ppsB VMRTAFSRISGMTAQQRTSLADEFDRVSRIAVAEPVAVVGIGCRFPGDVDGPESFWDFLVAGRNAISTVPADRWDAEAFYHPDPLTPGRMTTKWGGFVPDVAGFDAEFFGITPREAAAMDPQQRMLLEVAWEALEHAGIPPDSLGGTRTAVMMGVYFNEYQSMLAASPQNVDAYSGTGNAHSITVGRISYLLGLRGPAVAVDTACSSSLVAVHLACQSLRLRETDLALAGGVSITLRPETQIAISAWGLLSPQGRCAAFDAAADGFVRGEGAGVVVLKRLTDAVRDGDQVLAVVRGSAVNQDGRSNGVTAPNTAAQCDVIADALRSGDVAPDSVNYVEAHGTGTVLGDPIEFEALAATYGHGGDACALGAVKTNIGHLEAAAGIAGFIKATLAVQRATIPPNLHFSQWNPAIDAASTRFFVPTQNSPWPTAEGPRRAAVSSFGLGGTNAHVIIEQGSELAPVSEGGEDTGVSTLVVTGKTAQRMAATAQVLADWMEGPGAEVAVADVAHTVNHHRARQATFGTVVARDRAQAIAGLRALAAGQHAPGVVSHQDGSPGPGTVFVYSGRGSQWAGMGRQLLADEPAFAAAVAELEPVFVEQAGFSLRDVIATGKELVGIEQIQLGLIGMQLTLTELWRSYGVQPDLVIGHSMGEVAAAVVAGALTPAEGLRVTATRARLMAPLSGQGGMALLGLDAAATEALIADYPQVTVGIYNSPRQTVIAGPTEQIDELIARVRAQNRFASRVNIEVAPHNPAMDALQPAMRSELADLTPRTPTIGIISTTYADLHTQPIFDAEHWATNMRNPVRFQQAIASAGSGADGAYHTFIEISAHPLLTQAIADTLEDAHRPTKSAAKYLSIGTLQRDADDTVTFRTNLYTADIAHPPHTCHPPEPHPTIPTTPWQHTHHWIATTHPSTAAPEDPGSNKVVVNGQSTSESRALEDWCHQLAWPIRPAVSADPPSTAAWLVVADNELCHELARAADSRVDSLSPPALAAGSDPAALLDALRGVDNVLYAPPVPGELLDIESAYQVFHATRRLAAAMVASSATAISPPKLFIMTRNAQPISEGDRANPGHAVLWGLGRSLALEHPEIWGGIIDLDDSMPAELAVRHVLTAAHGTDGEDQVVYRSGARHVPRLQRRTLPGKPVTLNADASQLVIGATGNIGPHLIRQLARMGAKTIVAMARKPGALDELTQCLAATGTDLIAVAADATDPAAMQTLFDRFGTELPPLEGIYLAAFAGRPALLSEMTDDDVTTMFRPKLDALALLHRRSLKSPVRHFVLFSSVSGLLGSRWLAHYTATSAFLDSFAGARRTMGLPATVVDWGLWKSLADVQKDATQISAESGLQPMADEVAIGALPLVMNPDAAVATVVVAADWPLLAAAYRTRGALRIVDDLLPAPEDVGKGESEFRTSLRSCPAEKRRDMLFDHVGALAATVMGMPPTEPLDPSAGFFQLGMDSLMSVTLQRALSESLGEFLPASVVFDYPTVYSLTDYLATVLPELLEIGATAVATQQATDSYHELTEAELLEQLSERLRGTQ
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
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Chalut C et al. [2006]. The nonredundant roles of two 4'-phosphopantetheinyl transferases in vital processes of Mycobacteria. Biochemistry
- Walters SB et al. [2006]. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis. Transcriptome
- Niemann S, Koser CU, Gagneux S, Plinke C, Homolka S, Bignell H, Carter RJ, Cheetham RK, Cox A, Gormley NA, Kokko-Gonzales P, Murray LJ, Rigatti R, Smith VP, Arends FP, Cox HS, Smith G and Archer JA [2009]. Genomic diversity among drug sensitive and multidrug resistant isolates of Mycobacterium tuberculosis with identical DNA fingerprints. Sequence
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- Ioerger TR et al. [2010]. Variation among genome sequences of H37Rv strains of Mycobacterium tuberculosis from multiple laboratories. Sequence
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- 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