Gene Rv3804c (mpt44, 85A)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in cell wall mycoloylation. 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-a FbpA (mycolyl transferase 85A) (fibronectin-binding protein A) (antigen 85 complex A) |
| Comments | Rv3804c, (MT3911, MTV026.09c), len: 338 aa. FbpA (alternate gene names: mpt44, 85A), precursor of the 85-a antigen (fibronectin-binding protein A) (mycolyl transferase 85A) (see citations below), identical to P17944|P17996|FBPA|MPT44 antigen 85-a precursor from Mycobacterium bovis (338 aa), FASTA scores: opt: 2341, E(): 1.2e-132, (100.0% identity in 338 aa overlap); and highly similar to other Mycobacterial antigen precursors e.g. O52956|A85A_MYCAV|FBPA antigen 85-a precursor (85A) from Mycobacterium avium (347 aa), FASTA scores: opt: 1987, E(): 1.7e-111, (82.55% identity in 338 aa overlap); Q05861|A85A_MYCLE|FBPA|ML0097 antigen 85-a precursor (85A) from Mycobacterium leprae (330 aa), FASTA scores: opt: 1936, E(): 1.9e-108, (83.0% identity in 329 aa overlap); O06052|A85A_MYCGO|FBPA antigen 85-a precursor (85A) from Mycobacterium gordonae (339 aa), FASTA scores: opt: 1932, E(): 3.3e-108, (80.45% identity in 338 aa overlap); etc. Also highly similar to P31952|A85B_MYCTU|FBPB|Rv1886c|MT1934|MTCY180.32 secreted antigen 85-B from Mycobacterium tuberculosis (325 aa), FASTA scores: opt: 1830, E(): 3.9e-102, (78.85% identity in 317 aa overlap); P31953|A85C_MYCTU|FBPC|MPT45|Rv0129c|MTCI5.03c|FBPC2 secreted antigen 85-C from Mycobacterium tuberculosis (340 aa), FASTA scores: opt: 1597, E(): 3.4e-88, (67.25% identity in 336 aa overlap). Predicted possible vaccine candidate (See Zvi et al., 2008). |
| Functional category | Lipid metabolism |
| Proteomics | Corresponds to spots 3_494 and 3_496 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and spot 3804c 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 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry and Edman degradation (See Mattow et al., 2003). Identified in the cell wall fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). 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 | DNA microarrays and qRT-PCR show higher level of expression in M. tuberculosis H37Rv than in phoP|Rv0757 mutant (See Walters et al., 2006). |
| Mutant | 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). 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 | 4265642 | 4266658 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3804c|fbpA
MQLVDRVRGAVTGMSRRLVVGAVGAALVSGLVGAVGGTATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGANSPALYLLDGLRAQDDFSGWDINTPAFEWYDQSGLSVVMPVGGQSSFYSDWYQPACGKAGCQTYKWETFLTSELPGWLQANRHVKPTGSAVVGLSMAASSALTLAIYHPQQFVYAGAMSGLLDPSQAMGPTLIGLAMGDAGGYKASDMWGPKEDPAWQRNDPLLNVGKLIANNTRVWVYCGNGKPSDLGGNNLPAKFLEGFVRTSNIKFQDAYNAGGGHNGVFDFPDSGTHSWEYWGAQLNAMKPDLQRALGATPNTGPAPQGA
Bibliography
- Borremans M et al. [1989]. Cloning, sequence determination, and expression of a 32-kilodalton-protein gene of Mycobacterium tuberculosis. Secretion Product
- De Wit L et al. [1990]. Nucleotide sequence of the 32 kDa-protein gene (antigen 85 A) of Mycobacterium bovis BCG. Homolog Sequence
- Harth G et al. [1996]. Novel insights into the genetics, biochemistry, and immunocytochemistry of the 30-kilodalton major extracellular protein of Mycobacterium tuberculosis. Product
- 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
- 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
- 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
- Kremer L et al. [2002]. The M. tuberculosis antigen 85 complex and mycolyltransferase activity. Function
- 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. Secondary Mutant
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. 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
- 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
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. 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
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Walters SB et al. [2006]. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis. Transcriptome
- 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
- Zvi A et al. [2008]. Whole genome identification of Mycobacterium tuberculosis vaccine candidates by comprehensive data mining and bioinformatic analyses. Immunology
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- 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]. 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
