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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionInvolved 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].
ProductBifunctional protein polyribonucleotide nucleotidyltransferase GpsI: guanosine pentaphosphate synthetase + polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) (pnpase)
CommentsRv2783c, (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 categoryInformation pathways
ProteomicsIdentified 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).
MutantEssential 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
TypeStartEndOrientation
CDS30903393092597-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2783c|gpsI
MSAAEIDEGVFETTATIDNGSFGTRTIRFETGRLALQAAGAVVAYLDDDNMLLSATTASKNPKEHFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVDGLRNEIQIVVTILSLDPGDLYDVLAINAASASTQLGGLPFSGPIGGVRVALIDGTWVGFPTVDQIERAVFDMVVAGRIVEGDVAIMMVEAEATENVVELVEGGAQAPTESVVAAGLEAAKPFIAALCTAQQELADAAGKSGKPTVDFPVFPDYGEDVYYSVSSVATDELAAALTIGGKAERDQRIDEIKTQVVQRLADTYEGREKEVGAALRALTKKLVRQRILTDHFRIDGRGITDIRALSAEVAVVPRAHGSALFERGETQILGVTTLDMIKMAQQIDSLGPETSKRYMHHYNFPPFSTGETGRVGSPKRREIGHGALAERALVPVLPSVEEFPYAIRQVSEALGSNGSTSMGSVCASTLALLNAGVPLKAPVAGIAMGLVSDDIQVEGAVDGVVERRFVTLTDILGAEDAFGDMDFKVAGTKDFVTALQLDTKLDGIPSQVLAGALEQAKDARLTILEVMAEAIDRPDEMSPYAPRVTTIKVPVDKIGEVIGPKGKVINAITEETGAQISIEDDGTVFVGATDGPSAQAAIDKINAIANPQLPTVGERFLGTVVKTTDFGAFVSLLPGRDGLVHISKLGKGKRIAKVEDVVNVGDKLRVEIADIDKRGKISLILVADEDSTAAATDAATVTS
      
Bibliography