Gene Rv2783c
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Involved in mRNA degradation. Hydrolyses single-stranded polyribonucleotides processively in the 3' to 5' direction. Involved in the RNA degradosome, a multi-enzyme complex important in RNA processing and messenger RNA degradation [catalytic activity: RNA(N+1) + phosphate = RNA(N) + a nucleoside diphosphate]. |
Product | Bifunctional protein polyribonucleotide nucleotidyltransferase GpsI: guanosine pentaphosphate synthetase + polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) (pnpase) |
Comments | Rv2783c, (MTV002.48c), len: 752 aa. Probable gpsI, polyribonucleotide nucleotidyltransferase, equivalent to Q9CCF8|GPSI|ML0854 (alias O32966) putative polyribonucleotide phosphorylase / guanosine pentaphosphate synthetase from Mycobacterium leprae (773 aa), FASTA scores: opt: 4304, E(): 0, (89.95% identity in 757 aa overlap). Also highly similar to others e.g. O86656|GPSI guanosine pentaphosphate synthetase/ polyribonucleotide nucleotidyltransferase (fragment) from Streptomyces coelicolor (716 aa), FASTA scores: opt: 3393, E(): 5.8e-192, (72.77% identity in 718 aa overlap); Q53597|GPSI guanosine pentaphosphate synthetase from Streptomyces antibioticus (740 aa), FASTA scores: opt: 3314, E(): 2.6e-187, (70.55% identity in 733 aa overlap); P72659|PNP|SLL1043 polyribonucleotide nucleotidyltransferase from Synechocystis sp. strain PCC 6803 (718 aa), FASTA scores: opt: 1244, E(): 1.7e-65, (45.05% identity in 750 aa overlap); etc. Note that S. antibioticus guanosine pentaphosphate synthetase is a multifunctional enzyme that also acts as a polyribonucleotide nucleotidyltransferase. Start site chosen by homology from several alternatives. |
Functional category | Information pathways |
Proteomics | Identified by proteomics at the Statens Serum Institute (Denmark) (See Rosenkrands et al., 2000). 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 membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the aqueous phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-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 M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh 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). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011). |
Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). 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 | 3090339 | 3092597 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2783c|gpsI MSAAEIDEGVFETTATIDNGSFGTRTIRFETGRLALQAAGAVVAYLDDDNMLLSATTASKNPKEHFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVDGLRNEIQIVVTILSLDPGDLYDVLAINAASASTQLGGLPFSGPIGGVRVALIDGTWVGFPTVDQIERAVFDMVVAGRIVEGDVAIMMVEAEATENVVELVEGGAQAPTESVVAAGLEAAKPFIAALCTAQQELADAAGKSGKPTVDFPVFPDYGEDVYYSVSSVATDELAAALTIGGKAERDQRIDEIKTQVVQRLADTYEGREKEVGAALRALTKKLVRQRILTDHFRIDGRGITDIRALSAEVAVVPRAHGSALFERGETQILGVTTLDMIKMAQQIDSLGPETSKRYMHHYNFPPFSTGETGRVGSPKRREIGHGALAERALVPVLPSVEEFPYAIRQVSEALGSNGSTSMGSVCASTLALLNAGVPLKAPVAGIAMGLVSDDIQVEGAVDGVVERRFVTLTDILGAEDAFGDMDFKVAGTKDFVTALQLDTKLDGIPSQVLAGALEQAKDARLTILEVMAEAIDRPDEMSPYAPRVTTIKVPVDKIGEVIGPKGKVINAITEETGAQISIEDDGTVFVGATDGPSAQAAIDKINAIANPQLPTVGERFLGTVVKTTDFGAFVSLLPGRDGLVHISKLGKGKRIAKVEDVVNVGDKLRVEIADIDKRGKISLILVADEDSTAAATDAATVTS
Bibliography
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Parish T, Smith DA, Roberts G, Betts J and Stoker NG [2003]. The senX3-regX3 two-component regulatory system of Mycobacterium tuberculosis is required for virulence. Regulation
- 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
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. 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
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- 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]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- 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