Gene Rv2667 (clpX')
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Function unknown; possibly hydrolyzes peptides and/or proteins in presence of ATP. |
| Product | Possible ATP-dependent protease ATP-binding subunit ClpC2 |
| Comments | Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2, ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877, E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703|MTCY07H7B.26 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium tuberculosis (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); Q9S6T8|SCE94.24c putative CLP-family ATP-binding protease from Streptomyces coelicolor (841 aa), FASTA scores: opt: 303, E(): 5.6e-11, (38.8% identity in 152 aa overlap); etc. Some weak similarity to nearby P71961|MTCY441.33|Rv2664 hypothetical protein from Mycobacterium tuberculosis (83 aa). Contain Pfam match to entry PF02861 Clp amino terminal domain. Belongs to the CLPA/CLPB family. CLPC subfamily. Note that previously known as clpX' |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | Identified in the cytosol 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). |
| Transcriptomics | mRNA identified by microarray analysis and up-regulated after 24h and 96h of starvation (see citation below). |
| 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). 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 | 2983896 | 2984654 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2667|clpC2
MPEPTPTAYPVRLDELINAIKRVHSDVLDQLSDAVLAAEHLGEIADHLIGHFVDQARRSGASWSDIGKSMGVTKQAAQKRFVPRAEATTLDSNQGFRRFTPRARNAVVAAQNAAHGAASSEITPDHLLLGVLTDPAALATALLQQQEIDIATLRTAVTLPPAVTEPPQPIPFSGPARKVLELTFREALRLGHNYIGTEHLLLALLELEDGDGPLHRSGVDKSRAEADLITTLASLTGANAAGATDAGATDAG
Bibliography
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. 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
- 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
