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Search term: Rv2394

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nameggtB
Rv numberRv2394
TypeCDS
FunctionPlays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione [catalytic activity: 5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl-amino acid].
ProductProbable gamma-glutamyltranspeptidase precursor GgtB (gamma-glutamyltransferase) (glutamyl transpeptidase)
CommentsRv2394, (MTCY253.27c), len: 643 aa. Probable ggtB, gamma-glutamyltranspeptidase precursor, similar to many e.g. Q9KVF2|VC0194 from Vibrio cholerae (588 aa), FASTA scores: opt: 943, E(): 7.5e-47, (40.0% identity in 597 aa overlap); O69935|SC3C8.26 from Streptomyces coelicolor (603 aa), FASTA scores: opt: 822, E(): 7.2e-40, (33.6% identity in 622 aa overlap); P54422|GGT_BACSU from Bacillus subtilis (587 aa) FASTA scores: opt: 491, E(): 8.2e-21, (33.4% identity in 574 aa overlap); etc. Has potential signal peptide and appropriately positioned prokaryotic lipoprotein attachment site (PS00013).
Molecular mass (Da)66527.5
Isoelectric point5.9662
Gene length (bp)1932
Protein length643
Location (kb)2688.01


Functional categoryintermediary metabolism and respiration


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Putative glycoprotein identified by LC/ESI-MS/MS in the culture filtrate of M. tuberculosis H37Rv (See Gonzalez-Zamorano et al., 2009). 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 Kelkar 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
CDS26880102689941+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2394|ggtB
VSVWLRAGALVAAVMLSLSGCGGFHAGAPSTAGPCEIVPNGTPAPKTPPATVPSSRNLAT
NPEIATGYRRDMTVVRTAHYAAATANPLATQVACRVLRDGGTAADAVVAAQAVLGLVEPQ
SSGIGGGGYLVYFDARTGSVQAYDGREVAPAAATENYLRWVSDVDRSAPRPNARASGRSI
GVPGILRMLEMVHNEHGRTPWRDLFGPAVTLADGGFDISARMGAAISDAAPQLRDDPEAR
KYFLNPDGSPKPAGTRLTNPAYSKTLSAIASAGANAFYSGDIAHDIVAAASDTSNGRTPG
LLTIEDLAGYLAKRRQPLCTTYRGREICGMPSSGGVAVAATLGILEHFPMSDYAPSKVDL
NGGRPTVMGVHLIAEAERLAYADRDQYIADVDFVRLPGGSLTTLVDPGYLAARAALISPQ
HSMGSARPGDFGAPTAVAPPVPEHGTSHLSVVDSYGNAATLTTTVESSFGSYHLVDGFIL
NNQLSDFSAEPHATDGSPVANRVEPGKRPRSSMAPTLVFDHSSAGRGALYAVLGSPGGSM
IIQFVVKTLVAMLDWGLNPQQAVSLVDFGAANSPHTNLGGENPEINTSDDGDHDPLVQGL
RALGHRVNLAEQSSGLSAITRSEAGWAGGADPRREGAVMGDDA
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
PFAMP71750


Orthologs/Cross-references
CDC1551MT2464
Enzyme Classification2.3.2.2
Gene Ontologygamma-glutamyltransferase activity
acyltransferase activity
M. bovisMb2415
M. marinumMMAR_3713
M. smegmatisMSMEG_3076
UniProtP71750
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2394


Expression Data
TBDBRv2394


Bibliography
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
Xiong Y, Chalmers MJ, Gao FP, Cross TA, Marshall AG,
Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry.
J Proteome Res (2005) 4(3):855-61
Cited for: Proteomics
Gonzalez-Zamorano M, Mendoza-Hernandez G, Xolalpa W, Parada C, Vallecillo AJ, Bigi F, Espitia C,
Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins.
J Proteome Res (2009) 8(2):721-33
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, 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