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Search term: Rv1082

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namemca
Rv numberRv1082
TypeCDS
FunctionMycothiol-dependent detoxification enzyme, involved in mycothiol biosynthesis.
ProductMycothiol conjugate amidase Mca (mycothiol S-conjugate amidase)
CommentsRv1082, (MTV017.35), len: 288 aa. Mca, mycothiol conjugate amidase (see citation below), equivalent to NP_302547.1|NC_002677 conserved hypothetical protein from Mycobacterium leprae (290 aa), FASTA scores: opt: 1737, E(): 0, (86.4% identity in 287 aa overlap); and similar to Q54358|X79146 lmbE protein from Streptomyces lincolnensis (270 aa). Also similar to Rv1170|MTV005.06|MSHB GlcNAc-Ins deacetylase from Mycobacterium tuberculosis (303 aa), FASTA scores: opt: 411, E(): 9.4e-20, (35.8% identity in 299 aa overlap).
Molecular mass (Da)32699.7
Isoelectric point4.9277
Gene length (bp)867
Protein length288
Location (kb)1206.52


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 whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-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


Coordinates
TypeStartEndOrientation
RBS12065101206516+
CDS12065201207386+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1082|mca
VSELRLMAVHAHPDDESSKGAATLARYADEGHRVLVVTLTGGERGEILNPAMDLPDVHGR
IAEIRRDEMTKAAEILGVEHTWLGFVDSGLPKGDLPPPLPDDCFARVPLEVSTEALVRVV
REFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAGDFCRFPDAGEPWTVSKLYYVHGF
LRERMQMLQDEFARHGQRGPFEQWLAYWDPDHDFLTSRVTTRVECSKYFSQRDDALRAHA
TQIDPNAEFFAAPLAWQERLWPTEEFELARSRIPARPPETELFAGIEP
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
PFAMO53430


Orthologs/Cross-references
CDC1551MT1113
M. bovisMb1111
M. lepraeML2391
M. marinumMMAR_4385
M. smegmatisMSMEG_5261
UniProtO53430
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv1082


Expression Data
TBDBRv1082


Bibliography
Newton GL, Av-Gay Y, Fahey RC,
A novel mycothiol -dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase
Biochemistry (2000) 39(35):10739-46
Cited for: Product
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
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
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
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