Gene Rv3418c (cpn10, mpt57)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Binds to CPN60 in the presence of mg-ATP and suppresses the ATPase activity of the latter. |
| Product | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen) |
| Comments | Rv3418c, (MTCY78.11), len: 100 aa. GroES (alternate gene names: cpn10, mpt57), 10 kDa chaperonin (protein cpn10) (see citations below), equivalent to P24301|CH10_MYCLE|MOPB|GROES|CHPA|ML0380|B1620_C3_227|B229_C3_247 from Mycobacterium leprae (99 aa), FASTA scores: opt: 568, E(): 2.1e-31, (89.9% identity in 99 aa overlap). And also strongly identical to others e.g. O86017|CH10_MYCAV|MOPB|GROES from Mycobacterium avium and Mycobacterium paratuberculosis (99 aa), FASTA scores: opt: 611, E(): 2.9e-34, (96.95% identity in 99 aa overlap); P15020|CH10_MYCBO|MOPB|GROES from Mycobacterium bovis (99 aa), FASTA scores: opt: 596, E(): 2.9e-33, (98.95% identity in 94 aa overlap); P40172|CH10_STRCO|GROES|SC6G4.39 from Streptomyces coelicolor and Streptomyces lividans (102 aa), FASTA scores: opt: 480, E(): 1.6e-25, (76.75% identity in 99 aa overlap); etc. Also identical to MSG10KAG_1, MT10KAG_1, MTBCGA_1. Contains PS00681 Chaperonins cpn10 signature. Belongs to the GROES chaperonin family. |
| Functional category | Virulence, detoxification, adaptation |
| Proteomics | The product of this CDS corresponds to spots 5_154, 5_160, 5_157, 5_159 and 5_152 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations from 1999), and spots 3418c identified in short term culture filtrate, cell wall and cytosol by proteomics at the Statens Serum Institute (Denmark) (see proteomics citations from 2000). Identified in immunodominant fractions of both M. tuberculosis H37Rv culture filtrate and cytosol using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry and Edman degradation (See Mattow 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 culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified in the culture filtrate of M. tuberculosis H37Rv using LC-MS/MS; antigen recognized by serum pool from tuberculosis patients (See Malen et al., 2008). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (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 and up-regulated at high temperatures, and possibly down-regulated by hspR|Rv0353 and hrcA|Rv2374c (see Stewart et al., 2002). |
| Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019).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). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 3836986 | 3837288 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3418c|groES
VAKVNIKPLEDKILVQANEAETTTASGLVIPDTAKEKPQEGTVVAVGPGRWDEDGEKRIPLDVAEGDTVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK
Bibliography
- Baird PN et al. [1988]. A major antigen from Mycobacterium tuberculosis which is homologous to the heat shock proteins groES from E. coli and the htpA gene product of Coxiella burneti. Homolog Sequence
- Baird PN et al. [1989]. Cloning and sequence analysis of the 10 kDa antigen gene of Mycobacterium tuberculosis. Sequence
- Kong TH et al. [1993]. Mycobacterium tuberculosis expresses two chaperonin-60 homologs. Sequence Product
- Meghji S et al. [1997]. Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: a potential contributory factor in Pott's disease. Function
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- 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. [1999]. Differential T-cell recognition of native and recombinant Mycobacterium tuberculosis GroES. Product Function
- 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
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Taneja B et al. [2002]. Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution. Structure
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Mutant Regulation
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Roberts MM et al. [2003]. Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops. Structure
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Malen H, Softeland T and Wiker HG [2008]. Antigen analysis of Mycobacterium tuberculosis H37Rv culture filtrate proteins. Proteomics
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- 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
- 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
