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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
FunctionActs as a chaperone. Involved in induction by stress conditions e.g. heat shock. Possibly has an ATPase activity. Seems to be regulated positively by sigh (Rv3223c product) and negatively by HSPR (Rv0353 product).
ProductProbable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kDa protein) (HSP70)
CommentsRv0350, (MTCY13E10.10), len: 625 aa. Probable dnaK (alternate gene name: hsp70), 70 kDa heat shock protein (see citations below), equivalent to AAA25362.1|M95576|1924344A|738248 heat shock protein 70 from Mycobacterium leprae (621 aa); and DNAK_MYCPA|Q00488 (623 aa), FASTA scores: opt: 3678, E(): 0, (92.3% identity in 625 aa overlap). Also highly similar to others e.g. Q05558|DNAK_STRCO|453231|CAA54606.1|X77458 chaperone protein DNAK from Streptomyces coelicolor (618 aa). Has probably an ATPase activity. Note that this sequence differs from DNAK_MYCTU|P32723 (609 aa), due to a frameshift near the N-terminus. Belongs to the heat shock protein 70 family.
Functional categoryVirulence, detoxification, adaptation
ProteomicsThe product of this CDS corresponds to spots 1_447, 1_449, 1_450, 1_451 and 1_459 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and spots 0350 identified in short term culture filtrate, cell wall and cytosol by proteomics at the Statens Serum Institute (Denmark) (See Mollenkopf et al., 1999; Jungblut et al., 1999; Rosenkrands et al., 2000a, 2000b). Identified in immunodominant fractions of M. tuberculosis H37Rv culture filtrate 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 (See Mattow et al., 2003). Identified in the cytosol, cell wall, and cell membrane fractions of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the aqueous phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 2-DGE and MALDI-TOF-MS (See Sinha et al., 2005). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). 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 de Souza et al., 2011) (See Kelkar et al., 2011).
TranscriptomicsmRNA identified by RT-PCR in persistent bacteria at 37C; mRNA level increased at 45C (see Hu et al., 2000). mRNA also identified by DNA microarray analysis and highly 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). 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
CDS419835421712+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0350|dnaK
MARAVGIDLGTTNSVVSVLEGGDPVVVANSEGSRTTPSIVAFARNGEVLVGQPAKNQAVTNVDRTVRSVKRHMGSDWSIEIDGKKYTAPEISARILMKLKRDAEAYLGEDITDAVITTPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAALAYGLDKGEKEQRILVFDLGGGTFDVSLLEIGEGVVEVRATSGDNHLGGDDWDQRVVDWLVDKFKGTSGIDLTKDKMAMQRLREAAEKAKIELSSSQSTSINLPYITVDADKNPLFLDEQLTRAEFQRITQDLLDRTRKPFQSVIADTGISVSEIDHVVLVGGSTRMPAVTDLVKELTGGKEPNKGVNPDEVVAVGAALQAGVLKGEVKDVLLLDVTPLSLGIETKGGVMTRLIERNTTIPTKRSETFTTADDNQPSVQIQVYQGEREIAAHNKLLGSFELTGIPPAPRGIPQIEVTFDIDANGIVHVTAKDKGTGKENTIRIQEGSGLSKEDIDRMIKDAEAHAEEDRKRREEADVRNQAETLVYQTEKFVKEQREAEGGSKVPEDTLNKVDAAVAEAKAALGGSDISAIKSAMEKLGQESQALGQAIYEAAQAASQATGAAHPGGEPGGAHPGSADDVVDAEVVDDGREAK
      
Bibliography