Gene Rv2986c (hup, hlp, lbp21)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | This protein belongs to the histone like family of prokaryotic DNA-binding proteins which are capable of wrapping DNA to stabilize it, and prevent its denaturation under extreme environmental conditions. |
| Product | DNA-binding protein HU homolog HupB (histone-like protein) (HLP) (21-kDa laminin-2-binding protein) |
| Comments | Rv2986c, (MTCY349.01), len: 214 aa. hupB (alternate gene names: hup, hlp, lbp21), DNA-binding protein HU homolog (resembles fusion between HU and histone) (see Pethe et al., 2002), equivalent to others from Mycobacteria e.g. Q9XB18|DBH_MYCBO from Mycobacterium bovis (205 aa), FASTA scores: opt: 1050, E(): 5.6e-45, (95.35% identity in 214 aa overlap); Q9ZHC5|DBH_MYCSM from Mycobacterium smegmatis (208 aa), FASTA scores: opt: 1035, E(): 3.1e-44, (80.2% identity in 217 aa overlap); and O33125|DBH_MYCLE from Mycobacterium leprae (200 aa), FASTA scores: opt: 914, E(): 2.7e-38, (80.1% identity in 216 aa overlap). Also highly similar to others from other organisms e.g. O86537|DBH2_STRCO from Streptomyces coelicolor (218 aa), FASTA scores: opt: 569, E(): 2.6e-21, (51.35% identity in 220 aa overlap); P08821|DBH1_BACSU from Bacillus subtilis (92 aa), FASTA scores: opt: 280, E(): 2.5e-07, (45.05% identity in 91 aa overlap) (C-terminus shorter); etc. Contains PS00045 Bacterial histone-like DNA-binding proteins signature. Belongs to the bacterial histone-like protein family. Note that its C-terminal domain is very rich in lysine and alanine. |
| Functional category | Information pathways |
| Proteomics | 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 cell wall and cell membrane fractions of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011). |
| Transcriptomics | mRNA identified by microarray analysis and down-regulated after 96h of starvation (see Betts et al., 2002). DNA microarrays show increased expression in M. tuberculosis H37Rv in BALB/c mice compared to SCID mice, after 21 days of infection (See Talaat et al., 2004). |
| Mutant | 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 results in growth defect of H37Rv in vitro, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). 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 | 3343176 | 3343820 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2986c|hupB
MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK
Bibliography
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- Pethe K, Bifani P, Drobecq H, Sergheraert C, Debrie AS, Locht C and Menozzi FD [2002]. Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis. Product Function
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Talaat AM et al. [2004]. The temporal expression profile of Mycobacterium tuberculosis infection in mice. Transcriptome
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. 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
- 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
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- 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
