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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
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 2 ClpP2 (endopeptidase CLP 2)
CommentsRv2460c, (MT2535, MTV008.16c), len: 214 aa. Probable clpP2, ATP-dependent clp protease proteolytic subunit 2, equivalent to Q9CBY4|CLP2_MYCLE ATP-dependent CLP protease proteolytic subunit from Mycobacterium leprae (214 aa). Also highly similar to others e.g. Q9ZH58|CLPP2 from Streptomyces coelicolor (236 aa), FASTA scores: opt: 918, E(): 2.1e-50, (66.35% identity in 214 aa overlap); O67357|CLPP_AQUAE|AQ_1339 from Aquifex aeolicus (201 aa), FASTA scores: opt: 680, E(): 1.4e-35, (52.0% identity in 194 aa overlap); P43867|CLPP_HAEIN from Haemophilus influenzae (193 aa), FASTA scores: opt: 662, E(): 1.8e-34, (53.35% identity in 193 aa overlap); etc. Contains PS00381 Endopeptidase Clp serine active site. Also similar to upstream ORF Rv2461c|MTV008.17c|clpP1 (200 aa), FASTA score: (48.3% identity in 172 aa overlap). Belongs to peptidase family S14, also known as ClpP family. 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 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 membrane 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 and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011).
MutantEssential 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). 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
TypeStartEndOrientation
CDS27625312763175-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2460c|clpP2
VNSQNSQIQPQARYILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAVLLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLMETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLSAQTA
      
Bibliography