Gene Rv0475
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Required for extrapulmonary dissemination. Mediates adherence to epithelial cells by binding to sulfated glycoconjugates present at the surface of these cells; binds heparin, dextran sulfate, fucoidan and chondroitin sulfate. Promotes hemagglutination of erythrocytes of certain host species. Induces mycobacterial aggregation. |
| Product | Iron-regulated heparin binding hemagglutinin HbhA (adhesin) |
| Comments | Rv0475, hbhA (MTCY20G9.01), len: 199 aa. HbhA, iron-regulated heparin-binding hemagglutinin (see citations below), equivalent to CAC31971.1|AL583925 possible hemagglutinin from Mycobacterium leprae (188 aa). Contains possible N-terminal signal sequence and K-a-rich region at C-terminus: subcellular location: surface associated. A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al., 2004). |
| Functional category | Cell wall and cell processes |
| Proteomics | The product of this CDS has been identified by proteomics in the University of California (USA) (see Wong et al., 1999). 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 cytosol and cell wall 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 2-DGE and MALDI-TOF-MS (See Sinha 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 Kelkar et al., 2011). |
| Transcriptomics | mRNA identified by microarray analysis: transcription repressed at low pH in vitro conditions, which may mimic an environmental signal encountered by phagocytosed bacteria (see Fisher et al., 2002), and up-regulated at high temperatures (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). 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). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 565797 | 566396 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0475|hbhA
MAENSNIDDIKAPLLAALGAADLALATVNELITNLRERAEETRTDTRSRVEESRARLTKLQEDLPEQLTELREKFTAEELRKAAEGYLEAATSRYNELVERGEAALERLRSQQSFEEVSARAEGYVDQAVELTQEALGTVASQTRAVGERAAKLVGIELPKKAAPAKKAAPAKKAAPAKKAAAKKAPAKKAAAKKVTQK
Bibliography
- Menozzi FD, Rouse JH, Alavi M, Laude-Sharp M, Muller J, Bischoff R, Brennan MJ and Locht C [1996]. Identification of a heparin-binding hemagglutinin present in mycobacteria. Product Function Localization
- Menozzi FD et al. [1998]. Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin. Sequence Function
- Wong DK, Lee BY, Horwitz MA and Gibson BW [1999]. Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Proteomics Regulation
- Pethe K, Alonso S, Biet F, Delogu G, Brennan MJ, Locht C and Menozzi FD [2001]. The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Mutant Function
- Mueller-Ortiz SL et al. [2001]. Mycobacterial protein HbhA binds human complement component C3. Product Function
- Fisher MA, Plikaytis BB and Shinnick TM [2002]. Microarray analysis of the Mycobacterium tuberculosis transcriptional response to the acidic conditions found in phagosomes. Transcriptome Regulation
- Reddy VM, Masungi C, Hayworth DA, Temmerman S, Van Vooren JP, Drowart A, Pethe K, Menozzi FD, Locht C and Mascart F [2002]. Differential T and B cell responses against Mycobacterium tuberculosis heparin-binding hemagglutinin adhesin in infected healthy individuals and patients with tuberculosis. Product Function
- Pethe K, Bifani P, Drobecq H, Sergheraert C, Debrie AS, Locht C and Menozzi FD [2002]. Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis. Product Function
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Mutant Regulation
- 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
- Marmiesse M, Brodin P, Buchrieser C, Gutierrez C, Simoes N, Vincent V, Glaser P, Cole ST and Brosch R [2004]. Macro-array and bioinformatic analyses reveal mycobacterial 'core' genes, variation in the ESAT-6 gene family and new phylogenetic markers for the Mycobacterium tuberculosis complex. Homology
- 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
- 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
- Esposito C, Pethoukov MV, Svergun DI, Ruggiero A, Pedone C, Pedone E and Berisio R [2008]. Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis. Structure
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- 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
- 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
