Gene Rv0129c (mpt45, 85C, fbpC2)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity. |
| Product | Secreted antigen 85-C FbpC (85C) (antigen 85 complex C) (AG58C) (mycolyl transferase 85C) (fibronectin-binding protein C) |
| Comments | Rv0129c, (MT0137, MTCI5.03c), len: 340 aa. FbpC (alternate gene names: mpt45, 85C, fbpC2), secreted antigen 85c (fibronectin-binding protein C) (mycolyl transferase 85C) (see citations below), also highly similar to other Mycobacterial antigen precursors e.g. A85C_MYCLE|Q05862 antigen 85-c precursor (85c) from Mycobacterium leprae (333 aa), FASTA scores: opt: 1937, E(): 0, (81.4% identity in 333 aa overlap); etc. |
| Functional category | Lipid metabolism |
| Proteomics | The product of this CDS corresponds to spot 3_497 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and spot 0129c identified in short term culture filtrate by proteomics at the Statens Serum Institute (Denmark) (See Mollenkopf et al., 1999; Jungblut et al., 1999; Rosenkrands et al., 2000a, 2000b). 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry and Edman degradation (See Mattow et al., 2003). Predicted secreted protein - identified in culture filtrates of M. tuberculosis H37Rv; signal peptide predicted and cleavable signal sequence confirmed experimentally (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). 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). |
| Transcriptomics | mRNA identified by DNA microarray analysis (gene induced by isoniazid (INH) or ethionamide treatment) (see Wilson et al., 1999). |
| 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 and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 156578 | 157600 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0129c|fbpC
MTFFEQVRRLRSAATTLPRRLAIAAMGAVLVYGLVGTFGGPATAGAFSRPGLPVEYLQVPSASMGRDIKVQFQGGGPHAVYLLDGLRAQDDYNGWDINTPAFEEYYQSGLSVIMPVGGQSSFYTDWYQPSQSNGQNYTYKWETFLTREMPAWLQANKGVSPTGNAAVGLSMSGGSALILAAYYPQQFPYAASLSGFLNPSEGWWPTLIGLAMNDSGGYNANSMWGPSSDPAWKRNDPMVQIPRLVANNTRIWVYCGNGTPSDLGGDNIPAKFLEGLTLRTNQTFRDTYAADGGRNGVFNFPPNGTHSWPYWNEQLVAMKADIQHVLNGATPPAAPAAPAA
Bibliography
- Content J, de la Cuvellerie A, De Wit L, Vincent-Levy-Frebault V, Ooms J and de Bruyn J [1991]. The genes coding for the antigen 85 complexes of Mycobacterium tuberculosis and Mycobacterium bovis BCG are members of a gene family: cloning, sequence determination, and genomic organization of the gene coding for antigen 85-C of M. tuberculosis. Sequence
- Ohara N, Kitaura H, Hotokezaka H, Nishiyama T, Wada N, Matsumoto S, Matsuo T, Naito M and Yamada T [1995]. Characterization of the gene encoding the MPB51, one of the major secreted protein antigens of Mycobacterium bovis BCG, and identification of the secreted protein closely related to the fibronectin binding 85 complex. Homolog Secondary
- Belisle JT et al. [1997]. Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Function
- Chubb AJ, Woodman ZL, da Silva Tatley FM, Hoffmann HJ, Scholle RR and Ehlers MR [1998]. Identification of Mycobacterium tuberculosis signal sequences that direct the export of a leaderless beta-lactamase gene product in Escherichia coli. Secretion
- Wilson M, DeRisi J, Kristensen HH, Imboden P, Rane S, Brown PO and Schoolnik GK [1999]. Exploring drug-induced alterations in gene expression in Mycobacterium tuberculosis by microarray hybridization. Regulation
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Ronning DR et al. [2000]. Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Structure
- 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
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Puech V et al. [2002]. Evidence for a partial redundancy of the fibronectin-binding proteins for the transfer of mycoloyl residues onto the cell wall arabinogalactan termini of Mycobacterium tuberculosis. Mutant
- Kremer L et al. [2002]. The M. tuberculosis antigen 85 complex and mycolyltransferase activity. Function
- 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
- Dahl JL et al. [2003]. The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Regulon
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Ronning DR, Vissa V, Besra GS, Belisle JT and Sacchettini JC [2004]. Mycobacterium tuberculosis antigen 85A and 85C structures confirm binding orientation and conserved substrate specificity. Structure
- 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
- 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
- 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
