Gene Rv2623
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Function unknown |
| Product | Universal stress protein family protein TB31.7 |
| Comments | Rv2623, (MTCY01A10.09c), len: 297 aa. TB31.7, universal stress protein family protein, highly similar to hypothetical proteins from Mycobacterium tuberculosis e.g. Q10851|YK05_MYCTU|Rv2005c|MT2061|MTCY39.12 (295 aa), FASTA scores: opt: 1076, E(): 1.4e-60, (55.25% identity in 295 aa overlap); O53472|Rv2026c|MTV018.13c (294 aa), FASTA scores: opt: 988, E(): 4.8e-55, (51.5% identity in 295 aa overlap); Q10862|YJ96_MYCTU|Rv1996|MT2052|MTCY39.23c (317 aa), FASTA scores: opt: 688, E(): 4.1e-36, (45.1% identity in 315 aa overlap); etc. Also similar to several Streptomyces proteins e.g. Q9RIZ8|SCJ1.16c conserved hypothetical protein from Streptomyces coelicolor (294 aa), FASTA scores: opt: 407, E(): 2e-18, (32.65% identity in 303 aa overlap); and other bacterial hypothetical proteins e.g. Q9HPP5|VNG1536 from Halobacterium sp (147 aa), FASTA scores: opt: 180, E(): 0.00022, (31.65% identity in 139 aa overlap). Predicted possible vaccine candidate (See Zvi et al., 2008). Binds ATP. |
| Functional category | Virulence, detoxification, adaptation |
| Proteomics | The product of this CDS corresponds to spot TB31.7 identified in cell wall by proteomics at the Statens Serum Institute (Denmark), and at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations). Also identified in two-dimensional gel electrophoresis and by mass spectrometry, particularly in standing cultures (see Florczyk et al., 2001). Note that in Mycobacterium bovis BCG, proteome analysis by 2D-electrophoresis and MS identified this homologue which showed increased expression inside macrophages (see Monahan et al., 2001). Also identified at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see Rosenkrands et al., 2002). 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 cytosol and cell wall fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong 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 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 (gene induced by hypoxia) (see Sherman et al., 2001). |
| 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 H37Rv strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis Erdman Rv2623 mutant growth in vitro and in C57BL/6 mice is comparable to wild-type; mutant shows increased growth and virulence in Hartley guinea pigs and C3H/HeJ mice; Rv2623 overexpression results in reduced growth but not when ATP-binding ability is reduced (See Drumm et al., 2009). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 2949593 | 2950486 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2623|TB31.7
MSSGNSSLGIIVGIDDSPAAQVAVRWAARDAELRKIPLTLVHAVSPEVATWLEVPLPPGVLRWQQDHGRHLIDDALKVVEQASLRAGPPTVHSEIVPAAAVPTLVDMSKDAVLMVVGCLGSGRWPGRLLGSVSSGLLRHAHCPVVIIHDEDSVMPHPQQAPVLVGVDGSSASELATAIAFDEASRRNVDLVALHAWSDVDVSEWPGIDWPATQSMAEQVLAERLAGWQERYPNVAITRVVVRDQPARQLVQRSEEAQLVVVGSRGRGGYAGMLVGSVGETVAQLARTPVIVARESLT
Bibliography
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Sherman DR, Voskuil M, Schnappinger D, Liao R, Harrell MI and Schoolnik GK [2001]. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Transcriptome
- Monahan IM et al. [2001]. Differential expression of mycobacterial proteins following phagocytosis by macrophages. Homolog Proteomics
- Florczyk MA et al. [2001]. Identification and characterization of mycobacterial proteins differentially expressed under standing and shaking culture conditions, including Rv2623 from a novel class of putative ATP-binding proteins. Proteomics
- Rosenkrands I et al. [2002]. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. Proteomics Regulation
- Florczyk MA et al. [2003]. A family of acr-coregulated Mycobacterium tuberculosis genes shares a common DNA motif and requires Rv3133c (dosR or devR) for expression. Regulation Secondary
- Park HD et al. [2003]. Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Transcriptome
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Voskuil MI, Schnappinger D, Visconti KC, Harrell MI, Dolganov GM, Sherman DR and Schoolnik GK [2003]. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. Regulon
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Xiong Y, Chalmers MJ, Gao FP, Cross TA and Marshall AG [2005]. Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry. Proteomics
- Zvi A et al. [2008]. Whole genome identification of Mycobacterium tuberculosis vaccine candidates by comprehensive data mining and bioinformatic analyses. Immunology
- Drumm JE et al. [2009]. Mycobacterium tuberculosis universal stress protein Rv2623 regulates bacillary growth by ATP-Binding: requirement for establishing chronic persistent infection. Mutant Structure
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- Hingley-Wilson SM et al. [2010]. Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro. Homology
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- 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
