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Search term: Rv0126

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nametreS
Rv numberRv0126
FunctionInvolved in trehalose biosynthesis (protective effect). Converts maltose to trehalose. Mycobacteria can produce trehalose from glucose 6-phosphate and UDP-glucose (the OtsA-OtsB pathway) from glycogen-like alpha(1-->4)-linked glucose polymers (the TreY-TreZ pathway) and from maltose (the TreS pathway).
ProductTrehalose synthase TreS
CommentsRv0126, (MTCI418B.08), len: 601 aa. TreS, trehalose synthase (see citation below), highly similar to others e.g. CAA04601.2|AJ001205 putative trehalose synthase from Streptomyces coelicolor (566 aa); S71450|1536814|BAA11303.1|D78198 trehalose synthase maltose-specific from Pimelobacter sp. strain R48 (573 aa). Also similar to MAL1_DROME|P07191 possible maltase precursor (508 aa), FASTA scores: opt: 807, E(): 0, (33.7% identity in 504 aa overlap); and similar to proteins associated with amino-acid transport e.g. Q64319 rat protein which stimulates transport of cystine and dibasic and neutral amino acids (683 aa), FASTA scores: opt: 839, E(): 0, (32.0% identity in 531 aa overlap). Also similar to several other Mycobacterium tuberculosis proteins e.g. Rv2471 FASTA score: (31.7% identity in 164 aa overlap).
Molecular mass (Da)68593
Isoelectric point4.5821
Gene length (bp)1806
Protein length601
Location (kb)152.324

Functional categoryvirulence, detoxification, adaptation

ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). 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). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011).
Mutationslow growth mutant by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003) non essential gene by Himar1-based transposon mutagenesis in CDC1551 strain (see Lamichhane et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv0126|treS
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')

Structural information
Protein Data BankNo structure available

Enzyme Classification5.4.99.-
Gene Ontologycarbohydrate metabolic process
isomerase activity
cation binding
M. bovisMb0131
M. lepraeML2658
M. marinumMMAR_0325
M. smegmatisMSMEG_6515
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv0126

Expression Data

De Smet KA, Weston A, Brown IN, Young DB, Robertson BD,
Three pathways for trehalose biosynthesis in mycobacteria
Microbiology (2000) 146(1):199-208
Cited for: Function/Product/Biochemistry
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Lamichhane G, Zignol M, Blades NJ, Geiman DE, Dougherty A, Grosset J, Broman KW, Bishai WR,
A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2003) 100(12):7213-8
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Arntzen MO, Fortuin S, Schurch AC, Malen H, McEvoy CR, van Soolingen D, Thiede B, Warren RM, Wiker HG,
Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database.
Mol Cell Proteomics (2011) 10(1):M110.002527
Cited for: Proteomics/Sequence
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant