Gene Rv3417c (cpn60_1)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. |
| Product | 60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1) |
| Comments | Rv3417c, (MTCY78.12), len: 539 aa. GroEL1 (alternate genbe name: cpn60_1), 60 kDa chaperonin 1 (protein cpn60 1) (see citations below), equivalent to P37578|CH61_MYCLE|B1620_C3_228|GROL1|GROEL1|GROEL-1|GROE1|ML0381|B229_ 60 KDA chaperonin 1 from Mycobacterium leprae (537 aa), FASTA scores: opt: 2846, E(): 1.5e-154, (82.95% identity in 539 aa overlap). Also highly similar to others e.g. Q00767|CH61_STRAL|GROL1|GROEL1 from Streptomyces albus G (539 aa), FASTA scores: opt: 2130, E(): 8.1e-114, (61.9% identity in 541 aa overlap); P40171|CH61_STRCO|GROL1|GROEL1|SC6G4.40 from Streptomyces coelicolor (540 aa), FASTA scores: opt: 2119, E(): 3.4e-113, (61.8% identity in 542 aa overlap); etc. Also similar to P06806|CH62_MYCTU|Q48931|Rv0440|MTV037.04|GROL2|GROEL2|GROEL-2|HSP65 (62.2% identity in 527 aa overlap). Contains PS00017 ATP/GTP-binding site motif A, PS00296 Chaperonins cpn60 signature. Belongs to the chaperonin (HSP60) family. |
| Functional category | Virulence, detoxification, adaptation |
| Proteomics | Note that in Mycobacterium bovis BCG, proteome analysis by 2D-electrophoresis and MS identified this homolog which showed increased expression inside macrophages (see Mulder et al., 1997). Identified in carbonate extracts of M. tuberculosis H37Rv membranes using 2DGE and MALDI-MS (See Sinha 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 cell wall and cell membrane fractions 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 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 Kelkar et al., 2011). |
| Transcriptomics | mRNA identified by DNA microarray analysis and up-regulated at high temperatures, and possibly down-regulated by hrcA|Rv2374c (see Stewart et al., 2002). |
| 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 by Himar1 transposon mutagenesis in CDC1551 strain (see Lamichhane et al., 2003). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 3835272 | 3836891 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3417c|groEL1
MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAEDHDHHHGHAH
Bibliography
- Rinke de Wit TF, Bekelie S, Osland A, Miko TL, Hermans PW, van Soolingen D, Drijfhout JW, Schoningh R, Janson AA and Thole JE [1992]. Mycobacteria contain two groEL genes: the second Mycobacterium leprae groEL gene is arranged in an operon with groES. Function
- Kong TH et al. [1993]. Mycobacterium tuberculosis expresses two chaperonin-60 homologs. Sequence Product
- Mulder MA et al. [1997]. Mycobacterial promoters. Review Regulation
- Monahan IM et al. [2001]. Differential expression of mycobacterial proteins following phagocytosis by macrophages. Homolog Proteomics
- Lewthwaite JC, Coates AR, Tormay P, Singh M, Mascagni P, Poole S, Roberts M, Sharp L and Henderson B [2001]. Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain. Product Function
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Mutant Regulation
- Sinha S et al. [2002]. Proteome analysis of the plasma membrane of Mycobacterium tuberculosis. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- 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
- 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
- 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
