Gene Rv2224c
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Converts unknown esters to corresponding free acid and alcohol |
| Product | Probable carboxylesterase CaeA |
| Comments | Rv2224c, (MTCY427.05c), len: 520 aa. Probable caeA, carboxylesterase; has signal sequence and lipoprotein motif at N-terminal end. Very similar to three proteases/peptidases from Streptomyces spp.: L42758, L42759, L27466. FASTA score: L4 2758|STMSLPD STMSLPD NID: g940302 - Streptomyces (539 aa) opt: 1032 E(): 0, (37.5% identity in 533 aa overlap). Similar to hypothetical protein SW:YZZE_ECOLI P34211 (27.7% identity in 412 aa overlap) and highly similar to Rv2224c and Rv2672 (49.3% identity in 507 aa overlap); contains PS00013, Prokaryotic membrane lipoprotein lipid attachment site, and PS00120 Lipases, serine active site. Conserved in M. tuberculosis, M. leprae, M. bovis and M. avium paratuberculosis; predicted to be essential for in vivo survival and pathogenicity (See Ribeiro-Guimaraes and Pessolani, 2007). Predicted to be an outer membrane protein (See Song et al., 2008). |
| Functional category | Cell wall and cell processes |
| 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 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 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 level (identified by real-time quantitative RT-PCR) increased 24 and 72h after cultured macrophages infection (see citation below). |
| 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 and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Required for growth in C57BL/6J mouse spleen, by transposon site hybridization (TraSH) in H37Rv (See Sassetti and Rubin, 2003). Required for survival in primary murine macrophages, by transposon site hybridization (TraSH) in H37Rv (See Rengarajan et al., 2005). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis H37Rv transposon mutant is sensitive to pH 4.5 in 7H9 with Tween or Tyloxapol, but not phosphate-citrate buffer with Tyloxapol (See Vandal et al., 2008); mutant is mildly attenuated in C57BL/6 mice (See Vandal et al., 2009). M. tuberculosis H37Rv Rv2224c transposon mutant shows growth defect in C57BL/6 mice co-infected with mutant and wild-type; is attenuated in C57BL/6 and RAG -/- mice; is more susceptible to lysozyme; shows growth defect in C57BL/6 bone marrow macrophages and secretion of cytokines and chemokines is reduced (See Rengarajan et al., 2008). M. tuberculosis CDC1551 MT2282 (Rv2224c) mutant is attenuated in BALB/c mice (See Lun and Bishai, 2007). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 2495461 | 2497023 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2224c|caeA
VGMRLSRRDKIARMLLIWAALAAVALVLVGCIRVVGGRARMAEPKLGQPVEWTPCRSSNPQVKIPGGALCGKLAVPVDYDRPDGDVAALALIRFPATGDKIGSLVINPGGPGESGIEAALGVFQTLPKRVHERFDLVGFDPRGVASSRPAIWCNSDADNDRLRAEPQVDYSREGVAHIENETKQFVGRCVDKMGKNFLAHVGTVNVAKDLDAIRAALGDDKLTYLGYSYGTRIGSAYAEEFPQRVRAMILDGAVDPNADPIEAELRQAKGFQDAFNNYAADCAKNAGCPLGADPAKAVEVYHSLVDPLVDPDNPRISRPARTKDPRGLSYSDAIVGTIMALYSPNLWQHLTDGLSELVDNRGDTLLALADMYMRRDSHGRYNNSGDARVAINCVDQPPVTDRDKVIDEDRRAREIAPFMSYGKFTGDAPLGTCAFWPVPPTSQPHAVSAPGLVPTVVVSTTHDPATPYKAGVDLANQLRGSLLTFDGTQHTVVFQGDSCIDEYVTAYLIGGTTPPSGAKC
Bibliography
- Dubnau E et al. [2002]. Mycobacterium tuberculosis genes induced during infection of human macrophages. Transcriptome
- 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
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Sassetti CM and Rubin EJ [2003]. Genetic requirements for mycobacterial survival during infection. Mutant
- Rengarajan J et al. [2005]. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Mutant
- 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
- Ribeiro-Guimarães ML et al. [2007]. Comparative genomics of mycobacterial proteases. Homology
- Lun S et al. [2007]. Characterization of a novel cell wall-anchored protein with carboxylesterase activity required for virulence in Mycobacterium tuberculosis. Function Mutant Product
- Vandal OH et al. [2008]. A membrane protein preserves intrabacterial pH in intraphagosomal Mycobacterium tuberculosis. Mutant
- Rengarajan J et al. [2008]. Mycobacterium tuberculosis Rv2224c modulates innate immune responses. Mutant
- Song H, Sandie R, Wang Y, Andrade-Navarro MA and Niederweis M [2008]. Identification of outer membrane proteins of Mycobacterium tuberculosis. Localization
- Vandal OH et al. [2009]. Acid-susceptible mutants of Mycobacterium tuberculosis share hypersusceptibility to cell wall and oxidative stress and to the host environment. Mutant
- 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
