Gene Rv0934 (phoS1, phoS)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in active transport of inorganic phosphate across the membrane (import). This is one of the proteins required for binding-protein-mediated phosphate transport. |
| Product | Periplasmic phosphate-binding lipoprotein PstS1 (PBP-1) (PstS1) |
| Comments | Rv0934, (MTCY08D9.05c), len: 374 aa. PstS1 (previously known as phoS1 or phoS), phosphate-binding lipoprotein component of inorganic phosphate transport system (see citations below), highly similar to Rv0932c|MTCY08D9.07|pstS2 phosphate-binding periplasmic lipoprotein from Mycobacterium tuberculosis (370 aa), FASTA scores: opt: 460, E(): 5.9e-19, (31.2% identity in 375 aa overlap); and Rv0928|MTCY21C12.22|pstS3 phosphate-binding periplasmic lipoprotein from Mycobacterium tuberculosis (374 aa), FASTA scores: opt: 435, E():1.1e-17, (30.0% identity in 380 aa overlap) (Mycobacterium tuberculosis seems to have three PstS-like proteins, others being Rv0932c and Rv0928c). Also highly similar to MTCY08D9.05c|P15712|PAB_MYCTU protein antigen B precursor from Mycobacterium tuberculosis (374 aa), FASTA scores: opt: 2459, E(): 0, (100% identity in 374 aa overlap). Contains a prokaryotic membrane lipoprotein lipid attachment site (PS00013) at the N-terminus so the 23 aa leader peptide sequence is probably removed. Belongs to family of phosphate receptors for bacterial ABC-type lipoprotein transporters. |
| Functional category | Cell wall and cell processes |
| Proteomics | The product of this CDS corresponds to spot 0934 identified in short term culture filtrate by proteomics at the Statens Serum Institute (Denmark) (see proteomics citations). 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 Triton X-114 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 1-DGE and MALDI-TOF-MS (See Sinha et al., 2005). Predicted surface lipoprotein - identified in culture filtrates of M. tuberculosis H37Rv; signal peptide predicted (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). 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 M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh 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). |
| 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). 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
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 1042115 | 1043239 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0934|pstS1
VKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQVHFQPLPPAVVKLSDALIATISS
Bibliography
- Braibant M et al. [1996]. A Mycobacterium tuberculosis gene cluster encoding proteins of a phosphate transporter homologous to the Escherichia coli Pst system. Sequence
- Lefèvre P et al. [1997]. Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. Product
- Tanghe A et al. [1999]. Immunogenicity and protective efficacy of tuberculosis DNA vaccines encoding putative phosphate transport receptors. Product
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Braibant M et al. [2000]. The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. Review Secondary
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Torres A et al. [2001]. Molecular analysis of Mycobacterium tuberculosis phosphate specific transport system in Mycobacterium smegmatis. Characterization of recombinant 38 kDa (PstS-1). Regulation Secretion
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Sinha S et al. [2002]. Proteome analysis of the plasma membrane of Mycobacterium tuberculosis. Proteomics
- Vyas NK et al. [2003]. Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions. Structure
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- 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
- 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
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. 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
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Malen H, Softeland T and Wiker HG [2008]. Antigen analysis of Mycobacterium tuberculosis H37Rv culture filtrate proteins. 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
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- 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
