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Gene: pbpA

General annotation | Coordinates | Sequence | Genome Browser | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography


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General annotation
Gene namepbpA
Rv numberRv0016c
TypeCDS
FunctionINVOLVED IN PEPTIDOGLYCAN SYNTHESIS (AT THE FINAL STAGES). CELL WALL FORMATION; PBPA IS SUPPOSED TO BE RESPONSIBLE FOR THE DETERMINATION OF THE ROD SHAPE OF THE CELL. ITS SYNTHESIZES CROSS-LINKED PEPTIDOGLYCAN FROM LIPID INTERMEDIATES.
ProductPROBABLE PENICILLIN-BINDING PROTEIN PBPA
Evidenceexperimental
CommentsRv0016c, (MTCY10H4.16c), len: 491 aa. Probable pbpA, penicillin-binding protein, equivalent to NP_301144.1|NC_002677 putative penicillin-binding protein from Mycobacterium leprae (492 aa); and highly similar to MLCB1770_1 penicillin binding protein from Mycobacterium leprae (474 aa), FASTA scores: opt: 2516, E(): 0, (82.4% identity in 472 aa overlap). Also similar to others e.g. T36716 from Streptomyces coelicolor (490 aa); AAF61246.1|AF241575|PbpA from Streptomyces griseus (485 aa); NP_347146.1|NC_003030 from Clostridium acetobutylicum (482 aa); E235825|pbpA penicillin binding protein (325 aa), FASTA scores: opt: 1618, E(): 0, (78.3% identity in 323 aa overlap); etc. And also similar to MTCY270_5 and MTV003_8 from Mycobacterium tuberculosis.
Molecular mass (Da)51575.5
Isoelectric point8.5573
Gene length (bp)1476
Protein length491
Location (kb)20.234


Functional categorycell wall and cell processes


ProteomicsIdentified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005).
TranscriptomemRNA identified by microarray analysis and down-regulated after 4h, 24h and 96h of starvation (see Betts et al., 2002).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003) mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS1875920234-


Protein sequence in FASTA format
>M. tuberculosis H37Rv | pbpA
MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPN
PEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKG
AVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATET
EQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAE
STVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLT
ELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGR
AVIEAALQGEP
Blastp: results
TransMembrane prediction using Hidden Markov Models: tmhmm
Microbe Genome Browser
Genomic sequence

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Structural information
Protein Data BankNo structure available
PFAMProtein Family Domains


Orthologs/Cross-references
CDC1551MT0019
Gene Ontologyplasma membrane
cell wall organization
regulation of cell shape
penicillin binding
peptidoglycan biosynthetic process
integral to membrane
transferase activity
MbovisMb0016c
MlepraeML0018
MmarinumMMAR_0018
MsmegmatisMSMEG_0031
UniProtP71586


Interacting Drugs/Compounds
TDR TargetsRv0016c


Expression Data
TBDBRv0016c


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 :717
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
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 :7213
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404