Gene Rv2031c (acr) in Mycobacterium tuberculosis H37Rv
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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
Gene summary information
Gene namehspX
Gene length435 bp
IdentifierRv2031c
Location 2278498 bp
Protein summary information
Molecular mass16227.3 Da
Isoelectric point4.7523
Protein length144 amino acids
Structural information
PFAMP0A5B7
Orthologs
M. bovis AF2122-97Mb2057c
M. marinum MMMAR_3484
M. smegmatis MC2-155MSMEG_3932
M. tuberculosis 18bMT18B_2676
M. tuberculosis MTBC0mtbc0_002164
Cross-references
UniProtP9WMK1
Gene OntologyCytoplasm, Extracellular region, Cell wall
SWISS-MODELP9WMK1
TB databaseRv2031c
Interacting Drugs/Compounds
TDR TargetsLink
Precomputed results
BLASTReport
General annotation
TypeCDS
FunctionStress protein induced by anoxia. Has a proposed role in maintenance of long-term viability during latent, asymptomatic infections, and a proposed role in replication during initial infection. Regulated by the two component regulatory system DEVR|Rv3133c/DEVS|Rv3132c, in response to a hypoxic signal.
ProductHeat shock protein HspX (alpha-crystallin homolog) (14 kDa antigen) (HSP16.3)
CommentsRv2031c, (MTV018.18c), len: 144 aa. HspX, heat shock protein localized in the inner membrane (see citations below). Identical to P30223|14KD_MYCTU 14 KD antigen (16 kDa antigen) (HSP 16.3) of Mycobacterium tuberculosis (143 aa). Belongs to the small heat shock protein (HSP20) family. Also known as alpha-crystallin and gene as acr (see some citations below). Predicted possible vaccine candidate (See Zvi et al., 2008).
Functional categoryVirulence, detoxification, adaptation
ProteomicsThe product of this CDS corresponds to spots 5_85, 5_33, 5_141, 5_84, 5_89, 5_146, 5_238 and 5_66 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations from 1999), and spots 2031c identified in short term culture filtrate and cell wall by proteomics at the Statens Serum Institute (Denmark) (see proteomics citations from 2000). Identified 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). Also identified in two-dimensional gel electrophoresis and by mass spectrometry, particularly in standing cultures (see Florczyk et al., 2001). Also identified by proteomics in the University of California (USA) (see Wong et al., 1999) and upregulated during starvation (see Betts et al., 2002). Note that in Mycobacterium bovis BCG, proteome analysis by 2D-electrophoresis and MS identified this homolog which showed increased expression inside macrophages (see Monahan et al., 2001). Also identified at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see Rosenkrands et al., 2002). Identified in Triton X-114 and 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 and Edman degradation (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 CEGE 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 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 DNA microarray analysis: gene induced by hypoxia (see Sherman et al., 2001) and upregulated during starvation (see Betts et al., 2002). mRNA level (identified by real-time quantitative RT-PCR) increased only 6h after infection of cultured macrophages infection (see Dubnau et al., 2002). mRNA also identified by RT-PCR in stationary-phase and persistent bacteria (see Hu et al., 2000). RT-PCR shows increased expression in M. tuberculosis H37Rv grown in anaerobic non-replicating conditions (See Saxena et al., 2008).
MutantNon-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-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
CDS22784982278932-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2031c|hspX
MATTLPVQRHPRSLFPEFSELFAAFPSFAGLRPTFDTRLMRLEDEMKEGRYEVRAELPGVDPDKDVDIMVRDGQLTIKAERTEQKDFDGRSEFAYGSFVRTVSLPVGADEDDIKATYDKGILTVSVAVSEGKPTEKHIQIRSTN
Bibliography