Gene Rv0627
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Unknown |
Product | Possible toxin VapC5 |
Comments | Rv0627, (MTCY20H11.08), len: 135 aa. Possible vapC5, toxin, part of toxin-antitoxin (TA) operon with Rv0626, contains PIN domain (See Arcus et al., 2005; Pandey and Gerdes, 2005). Similar to others in Mycobacterium tuberculosis e.g. Rv0595c and Rv0665. |
Functional category | Virulence, detoxification, adaptation |
Proteomics | 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). |
Mutant | essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Check for mutants available at TARGET website |
Coordinates
Type | Start | End | Orientation |
---|---|---|---|
CDS | 718282 | 718689 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0627|vapC5 VSTTPAAGVLDTSVFIATESGRQLDEALIPDRVATTVVTLAELRVGVLAAATTDIRAQRLATLESVADMETLPVDDDAARMWARLRIHLAESGRRVRINDLWIAAVAASRALPVITQDDDFAALDGAASVEIIRV
Bibliography
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Arcus VL et al. [2005]. The PIN-domain toxin-antitoxin array in mycobacteria. Biochemistry
- Pandey DP et al. [2005]. Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Homology
- Gupta A [2009]. Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. Function
- Ramage HR, Connolly LE and Cox JS [2009]. Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. Function
- Miallau L et al. [2009]. Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. Structure
- 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