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Search term: Rv2903c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namelepB
Rv numberRv2903c
TypeCDS
FunctionCleavage of N-terminal leader sequences from secreted protein precursors.
ProductProbable signal peptidase I LepB (SPASE I) (leader peptidase I).
CommentsRv2903c, (MTCY274.34c), len: 294 aa. Probable lepB, signal peptidase I (type II membrane protein) (see Braunstein & Belisle 2000), equivalent to O33021|LEP_MYCLE|ML1612|MLCB250.39 probable signal peptidase I from Mycobacterium leprae (289 aa), FASTA scores: opt: 1335, E(): 1.8e-77, (69.75% identity in 301 aa overlap). Also similar to many e.g. O86869|SIPX signal peptidase I from Streptomyces lividans (320 aa), FASTA scores: opt: 474, E(): 1e-22, (43.55% identity in 248 aa overlap); O69884|SIP1|SIPW putative signal peptidase I from Streptomyces coelicolor and Streptomyces lividans (259 aa), FASTA scores: opt: 226, E(): 5e-07, (36.0% identity in 214 aa overlap); P42668|LEP_BACLI|sip signal peptidase I from Bacillus licheniformis (186 aa), FASTA scores: opt: 218, E(): 1.3e-06, (34.5% identity in 194 aa overlap); etc. Contains PS00501 Signal peptidases I serine active site,and PS00761 Signal peptidases I signature 3. Belongs to peptidase family S26; also known as type I leader peptidase family. Conserved in M. tuberculosis, M. leprae, M. bovis and M. avium paratuberculosis; predicted to be essential for in vivo survival and pathogenicity (See Ribeiro-Guimaraes and Pessolani, 2007).
Molecular mass (Da)31848.2
Isoelectric point5.7282
Gene length (bp)885
Protein length294
Location (kb)3212.97


Functional categorycell wall and cell processes


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS; predicted integral membrane protein (See Xiong 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 membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011).
TranscriptomemRNA identified by microarray analysis and down-regulated after 24h and 96h of starvation (see Betts et al., 2002).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti 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
RegulonPredicted to be in the RelA|Rv2583c regulon (See Dahl et al., 2003).


Coordinates
TypeStartEndOrientation
CDS32129703213854-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2903c|lepB
VTETTDSPSERQPGPAEPELSSRDPDIAGQVFDAAPFDAAPDADSEGDSKAAKTDEPRPA
KRSTLREFAVLAVIAVVLYYVMLTFVARPYLIPSESMEPTLHGCSTCVGDRIMVDKLSYR
FGSPQPGDVIVFRGPPSWNVGYKSIRSHNVAVRWVQNALSFIGFVPPDENDLVKRVIAVG
GQTVQCRSDTGLTVNGRPLKEPYLDPATMMADPSIYPCLGSEFGPVTVPPGRVWVMGDNR
THSADSRAHCPLLCTDDPLPGTVPVANVIGKARLIVWPPSRWGVVRSVNPQQGR
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
PFAMQ10789


Orthologs/Cross-references
CDC1551MT2971
Enzyme Classification3.4.21.89
Gene Ontologyplasma membrane
proteolysis
serine-type peptidase activity
integral to membrane
M. bovisMb2927c
M. lepraeML1612
M. marinumMMAR_1805
M. smegmatisMSMEG_2441
UniProtQ10789
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2903c


Expression Data
TBDBRv2903c


Bibliography
Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K,
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Mol Microbiol (2002) 43(3):717-31
Cited for: Transcriptome
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
Dahl JL, Kraus CN, Boshoff HI, Doan B, Foley K, Avarbock D, Kaplan G, Mizrahi V, Rubin H, Barry CE 3rd,
The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice.
Proc Natl Acad Sci U S A (2003) 100(17):10026-31
Cited for: Regulon
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
Ribeiro-Guimaraes ML, Pessolani MC,
Comparative genomics of mycobacterial proteases.
Microb Pathog (2007) 43(5-6):173-8
Cited for: Homology
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
Kruh NA, Troudt J, Izzo A, Prenni J, Dobos KM,
Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo.
PLoS One (2010) 5(11):e13938
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
Braunstein M, Belisle JT,
Molecular Genetics of Mycobacteria; Thirteenth chapter: Genetics of Protein Secretion
ASM Press (2000) 1-55581-191-4:203-220
Cited for: Review