Gene Rv0815c (sseC4)
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | May be a sulfotransferase involved in the formation of thiosulfate [catalytic activity: thiosulfate + cyanide = sulfite + thiocyanate]. |
Product | Probable thiosulfate sulfurtransferase CysA2 (rhodanese-like protein) (thiosulfate cyanide transsulfurase) (thiosulfate thiotransferase) |
Comments | Rv0815c, (MTV043.07c, MT0837, O05793), len: 277 aa. Probable cysA2 (alternate gene name: sseC4), thiosulfate sulfurtransferase (see Wooff et al., 2002), equivalent to Q50036|CYSA|CYSA3|ML2198|THTR_MYCLE putative sulfurtransferase thiosulfate from Mycobacterium leprae (277 aa). Also highly similar to other putative thiosulfate sulfurtransferases e.g. P16385|THTR_SACER putative thiosulfate sulfurtransferase from Saccharopolyspora erythraea (Streptomyces erythraeus) (281 aa); NP_293941.1|NC_001263 thiosulfate sulfurtransferase from Deinococcus radiodurans (286 aa); etc. Identical second copy present as Rv3117|MTCY164.27|MT3199|O05793|cysA3 (277 aa) (100.0% identity in 277 aa overlap). Contains PS00683 Rhodanese C-terminal signature at C-terminus. Belongs to the rhodanese family. |
Functional category | Intermediary metabolism and respiration |
Proteomics | Identified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, and possibly identified in two-dimensional gel electrophoresis and by mass spectrometry in standing cultures (see proteomics citations). 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in the cytosol and cell wall fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega 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). |
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 CDC1551 strain (see Lamichhane 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 | 908485 | 909318 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0815c|cysA2 MARCDVLVSADWAESNLHAPKVVFVEVDEDTSAYDRDHIAGAIKLDWRTDLQDPVKRDFVDAQQFSKLLSERGIANEDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASPPDNTIRAFRDEVLAAINVKNLIDVRSPDEFSGKILAPAHLPQEQSQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRELLGHQNVKNYDGSWTEYGSLVGAPIELGS
Bibliography
- 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 et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Florczyk MA et al. [2001]. Identification and characterization of mycobacterial proteins differentially expressed under standing and shaking culture conditions, including Rv2623 from a novel class of putative ATP-binding proteins. Proteomics
- Wooff E et al. [2002]. Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Homolog Mutant Function
- 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
- 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
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- MÃ¥len 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
- 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
- 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