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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
FunctionBinds to CPN60 in the presence of mg-ATP and suppresses the ATPase activity of the latter.
Product10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen)
CommentsRv3418c, (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 categoryVirulence, detoxification, adaptation
ProteomicsThe 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).
TranscriptomicsmRNA 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).
MutantEssential 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
TypeStartEndOrientation
CDS38369863837288-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3418c|groES
VAKVNIKPLEDKILVQANEAETTTASGLVIPDTAKEKPQEGTVVAVGPGRWDEDGEKRIPLDVAEGDTVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK
      
Bibliography