Gene Rv3841
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in iron storage; ferritin is an intracellular molecule that stores iron in a soluble, nontoxic, readily available form. The functional molecule, which is composed of 24 chains, is roughly spherical and contains a central cavity in which the polymeric ferric iron core is deposited. |
| Product | Bacterioferritin BfrB |
| Comments | Rv3841, (MTCY01A6.28c), len: 181 aa. bfrB, bacterioferritin, similar to other ferritin or hypothetical proteins e.g. O26261|MTH158|RSGA ferritin like protein from Methanothermobacter thermautotrophicus (171 aa), FASTA scores: opt: 277, E(): 6.6e-11, (30.1% identity in 166 aa overlap); Q99SZ3|SA1709 hypothetical protein from Staphylococcus aureus subsp. aureus N315 (166 aa), FASTA scores: opt: 275, E(): 8.7e-11, (33.35% identity in 156 aa overlap); Q9X0L2|TM1128 ferritin from Thermotoga maritima (164 aa), FASTA scores: opt: 247, E(): 5.3e-09, (25.65% identity in 156 aa overlap); Q9KDT7|BH1124 ferritin from Bacillus halodurans (169 aa), FASTA scores: opt: 246, E(): 6.3e-09, (28.95% identity in 152 aa overlap); O29424|AF0834 putative ferritin from Archaeoglobus fulgidu (169 aa), FASTA scores: opt: 246, E(): 6.3e-09, (28.95% identity in 152 aa overlap); etc. Also shows similarity with Rv1876|MTCY180.42|BFRA probable bacterioferritin from Mycobacterium tuberculosis (159 aa). Seems belong to the bacterioferritin family. |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | Identified at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see Rosenkrands et al., 2000). 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 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 in the aqueous phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-DGE, 2-DGE, and MALDI-TOF-MS (See Sinha et al., 2005). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Putative glycoprotein identified by LC/ESI-MS/MS in the culture filtrate of M. tuberculosis H37Rv (See Gonzalez-Zamorano et al., 2009). 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). |
| Transcriptomics | mRNA identified by microarray analysis: gene induced by hypoxia (see Sherman et al., 2001). DNA microarrays indicate induction by iron and IdeR|Rv2711 in M. tuberculosis H37Rv (See Rodriguez et al., 2002). Up-regulated at high temperatures and possibly down-regulated by hspR|Rv0353 (see Stewart et al., 2002). |
| Mutant | Non-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). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 4314178 | 4314723 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3841|bfrB
MTEYEGPKTKFHALMQEQIHNEFTAAQQYVAIAVYFDSEDLPQLAKHFYSQAVEERNHAMMLVQHLLDRDLRVEIPGVDTVRNQFDRPREALALALDQERTVTDQVGRLTAVARDEGDFLGEQFMQWFLQEQIEEVALMATLVRVADRAGANLFELENFVAREVDVAPAASGAPHAAGGRL
Bibliography
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Sherman DR, Voskuil M, Schnappinger D, Liao R, Harrell MI and Schoolnik GK [2001]. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Transcriptome
- Gold B et al. [2001]. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Regulon
- Rosenkrands I et al. [2002]. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. Proteomics Regulation
- Rodriguez GM, Voskuil MI, Gold B, Schoolnik GK and Smith I [2002]. ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Transcriptome
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Mutant Regulation
- Park HD et al. [2003]. Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Transcriptome
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Xiong Y, Chalmers MJ, Gao FP, Cross TA and Marshall AG [2005]. Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry. Proteomics
- Sinha S, Kosalai K, Arora S, Namane A, Sharma P, Gaikwad AN, Brodin P and Cole ST [2005]. Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics. Proteomics
- Prakash P et al. [2005]. Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames. Regulon
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- González-Zamorano M et al. [2009]. Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins. Proteomics
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- McMath LM et al. [2010]. Crystallization and preliminary X-ray crystallographic analysis of a Mycobacterium tuberculosis ferritin homolog, BfrB. Structure
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
