Rv0016c - penicillin-binding protein pbpA


Protein Domains

Gene Information
LocusRv0016c
SymbolpbpA
Gene Namepenicillin-binding protein pbpA
Location18759 - 20234 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1476 bp
Protein:492 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number35649
Related GenesAcel_0020 CE0035 cg0060 DIP0055 jk0039 MAP0019c MAV_0020 Mkms_0025 ML0018 Mmcs_0017 MSMEG_0031 MT0019 MUL_0020 Mvan_0025 nfa820 SAV4339
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv0016c
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionSignaling Rv2145cactivesourish102012-10-05
yeast-two-or-three hybrid (physical interaction)
P. Mukherjee, K. Sureka et al. Novel role of Wag31 in protection of mycobacteria under oxidative stress. Mol. Microbiol. 2009
InteractionSignaling Rv2145cactiveahal47892012-10-05
yeast-two-or-three hybrid (physical interaction)
P. Mukherjee, K. Sureka et al. Novel role of Wag31 in protection of mycobacteria under oxidative stress. Mol. Microbiol. 2009
InteractionPhysicalInteraction Rv0050activesinghpankaj21162012-10-05
Band Shift
authors,H. Billman-Jacobe,RE. Haites,RL. Coppel Characterization of a Mycobacterium smegmatis mutant lacking penicillin binding protein 1. Antimicrob. Agents Chemother. 1999
InteractionPhysicalInteraction Rv0050activesinghpankaj21162012-10-05
Band Shift
A. Fedarovich,RA. Nicholas,C. Davies Unusual conformation of the SxN motif in the crystal structure of penicillin-binding protein A from Mycobacterium tuberculosis. J. Mol. Biol. 2010
InteractionPhysicalInteraction Rv0050activesinghpankaj21162012-10-05
Band Shift
authors,M. Strong,TG. Graeber,M. Beeby,M. Pellegrini,MJ. Thompson,TO. Yeates,D. Eisenberg Visualization and interpretation of protein networks in Mycobacterium tuberculosis based on hierarchical clustering of genome-wide functional linkage maps. Nucleic Acids Res. 2003
InteractionRegulatory Rv0017cactivevmevada1022012-10-05
Functional linkage (operon)
authors,H. Matsuzawa,S. Asoh,K. Kunai,K. Muraiso,A. Takasuga,T. Ohta Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon. J. Bacteriol. 1989
InteractionRegulatory Rv0017cactivevmevada1022012-10-05
Functional linkage (operon)
A. Dasgupta, P. Datta et al. The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. Microbiology (Reading, Engl.) 2006
InteractionActivation Rv0014cactivevmevada1022012-10-05
Co-expression (Functional linkage)
A. Dasgupta, P. Datta et al. The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. Microbiology (Reading, Engl.) 2006
InteractionSignaling Rv0014cactivevmevada1022012-10-05
Co-expression (Functional linkage)
A. Narayan, P. Sachdeva et al. Serine threonine protein kinases of mycobacterial genus: phylogeny to function. Physiol. Genomics 2007
InteractionSignaling Rv0014cactivevmevada1022012-10-05
Co-expression (Functional linkage)
A. Dasgupta, P. Datta et al. The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. Microbiology (Reading, Engl.) 2006
NameClass B penicillin binding proteinactivemjackson2012-10-05
Cell division
NameClass B penicillin binding proteinactivemjackson2012-10-05
Cell division