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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
FunctionThis protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
ProductProbable iron-regulated elongation factor TU Tuf (EF-TU)
CommentsRv0685, (MTCY210.02), len: 396 aa. Probable tuf, iron-regulated elongation factor EF-Tu, equivalent to JC2262 translation elongation factor Tu from Mycobacterium leprae (396 aa). Also highly similar to others e.g. P42439|EFTU_CORGL elongation factor TU (EF-TU) from Corynebacterium glutamicum (396 aa); etc. Contains PS00017 ATP/GTP-binding site motif A, and PS00301 GTP-binding elongation factors signature. Belongs to the GTP-binding elongation factor family, EF-TU/EF-1A subfamily. Predicted possible vaccine candidate (See Zvi et al., 2008).
Functional categoryInformation pathways
ProteomicsThe product of this CDS corresponds to spots 1_367, 1_362, 1_171 and 1_349 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, spot 0685 (or EF-tu) identified in cell wall by proteomics at the Statens Serum Institute (Denmark), and spot identified in the University of California (USA) (see citations below). Note that in Mycobacterium bovis BCG, proteome analysis by 2D-electrophoresis and MS identified this homolog which showed increased expression inside macrophages (see citation below). 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 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 membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Identified in the detergent phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-DGE and MALDI-TOF-MS (See Sinha 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).
TranscriptomicsDNA microarrays show lower level of expression in M. tuberculosis H37Rv during Mg2+ starvation (See Walters et al., 2006).
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
CDS784821786011+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0685|tuf
VAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELLAAQEFDEDAPVVRVSALKALEGDAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVGIRPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK
      
Bibliography