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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
intermediary metabolism and respiration
regulatory proteins
conserved hypotheticals
lipid metabolism
General annotation
FunctionCLP cleaves peptides in various proteins in a process that requires ATP hydrolysis. CLP may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates.
ProductProbable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP)
CommentsRv2461c, (MT2536, MTV008.17c), len: 200 aa. Probable clpP1, ATP-dependent clp protease proteolytic subunit 1, equivalent to Q9CBY3|CLP1_MYCLE ATP-dependent CLP protease proteolytic subunit from Mycobacterium leprae (224 aa), FASTA scores: opt: 1226, E(): 1.3e-71, (95.0% identity in 200 aa overlap). Also highly similar to others e.g. Q9F315|CLPP1 from Streptomyces coelicolor (219 aa), FASTA scores: opt: 713, E(): 9.3e-39, (61.75% identity in 183 aa overlap); P80244|CLPP_BACSU from Bacillus subtilis (197 aa), FASTA scores: opt: 658, E(): 2.8e-35, (54% identity in 187 aa overlap); Q9WZF9|CLPP_THEMA|TM0695 from Thermotoga maritima (203 aa), FASTA scores: opt: 653, E(): 6.1e-35, (55.25% identity in 172 aa overlap); etc. Also similar to downstream ORF Rv2460c|MTV008.16c|clpP2 (214 aa), FASTA score: (48.3% identity in 172 aa overlap). Belongs to peptidase family S14, also known as CLPP family. Note that previously known as clp. Conserved in M. tuberculosis, M. leprae, M. bovis and M. avium paratuberculosis; predicted to be essential for in vivo survival and pathogenicity (See Ribeiro-Guimaraes and Pessolani, 2007).
Functional categoryIntermediary metabolism and respiration
ProteomicsIdentified in immunodominant fractions of M. tuberculosis H37Rv cytosol using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). 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 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 M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh 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).
MutantEssential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2461c|clpP1