Gene Rv0931c (mbk)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in signal transduction (via phosphorylation). Thought to regulate phosphate transport. Can phosphorylate the peptide substrate myelin basic protein (MBP) at serine and threonine residues. Can be autophosphorylated on threonine residues [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. |
| Product | Transmembrane serine/threonine-protein kinase D PknD (protein kinase D) (STPK D) |
| Comments | Rv0931c, (MTCY08D9.08), len: 664 aa. PknD (alternate gene name: mbk), transmembrane serine/threonine protein kinase (see citations below), equivalent to CAB62227.1|AJ250200 putative serine/threonine protein kinase from Mycobacterium bovis BCG (291 aa); and highly similar in N-terminus to P54744|PKNB_MYCLE probable serine/threonine-specific protein kinase from Mycobacterium leprae (622 aa). Also highly similar to others, particularly in N-terminal half e.g. NP_243370.1|NC_002570 serine/threonine protein kinase from Bacillus halodurans (664 aa); NP_268044.1|NC_002662 serine/threonine protein kinase from Lactococcus lactis (627 aa); etc. Also highly similar to other serine/threonine protein kinases from Mycobacterium tuberculosis e.g. pknH (626 aa), FASTA scores: opt: 1398, E: 0, (49.3% identity in 540 aa overlap); pknE (566 aa); pknB (626 aa); Rv3524 (343 aa); etc. Contains Hank's kinase subdomain. Contains two transmembrane segments, which flank a highly repetitive region, suggesting a receptor-like anchoring. Belongs to the Ser/Thr family of protein kinases. Experimental studies show evidence of auto-phosphorylation on a serine residue. Appears to be co-transcribed with Rv0932c|pstS2. |
| Functional category | Regulatory proteins |
| Proteomics | Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS; predicted transmembrane protein (See Gu 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; predicted integral membrane protein (See Xiong 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). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011). |
| Transcriptomics | mRNA identified by microarray analysis and down-regulated after 24h and 96h of starvation (see Betts 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). Disruption of this gene provides a growth advantage 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). M. tuberculosis CDC1551 transposon mutant is attenuated in the central nervous system of BALB/c mice (See Be et al., 2008). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 1037920 | 1039914 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0931c|pknD
VSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWAVVGAAAIVLVAIVAAAGYLVLRPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS
Bibliography
- Peirs P et al. [1997]. A serine/threonine protein kinase from Mycobacterium tuberculosis. Product Sequence Biochemistry
- Av-Gay Y et al. [2000]. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Review
- Peirs P et al. [2000]. The Mycobacterium bovis homologous protein of the Mycobacterium tuberculosis serine/threonine protein kinase Mbk (PknD) is truncated. Product
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- 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
- Good MC et al. [2004]. Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller. Structure
- 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
- Greenstein AE et al. [2007]. M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. Biochemistry
- Be NA et al. [2008]. Murine model to study the invasion and survival of Mycobacterium tuberculosis in the central nervous system. Mutant
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- 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
