Gene Rv2911 (dacB)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in peptidoglycan synthesis (at final stages). Hydrolyzes the bound D-alanyl-D-alanine [catalytic activity: D-alanyl-D-alanine + H(2)O = 2 D-alanine]. |
| Product | Probable penicillin-binding protein DacB2 (D-alanyl-D-alanine carboxypeptidase) (DD-peptidase) (DD-carboxypeptidase) (PBP) (DD-transpeptidase) (serine-type D-ala-D-ala carboxypeptidase) (D-amino acid hydrolase) |
| Comments | Rv2911, (MTCY274.43), len: 291 aa. Probable dacB2, D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein), an ala-rich protein. Highly similar (except in N-terminus) to Q9CCM2|ML0691 putative D-alanyl-D-alanine carboxypeptidase from Mycobacterium leprae (411 aa), FASTA scores: opt: 749, E(): 9.3e-39, (46.75% identity in 276 aa overlap). Also similar to penicillin binding proteins / D-alanyl-D-alanine carboxypeptidases e.g. Q9KCJ8|SC4G1.16c D-alanyl-D-alanine carboxypeptidase from Streptomyces coelicolor (382 aa), FASTA scores: opt: 386, E(): 2.1e-16, (31.25% identity in 285 aa overlap); P35150|DACB_BACSU penicillin-binding protein 5* precursor from Bacillus subtilis (382 aa), FASTA scores: opt: 384, E(): 3.6e-17, (30.7% identity in 244 aa overlap); Q9K8X5|DACB|BH2877 D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5) from Bacillus halodurans (395 aa), FASTA scores: opt: 359, E(): 9.7e-15, (30.3% identity in 241 aa overlap); P33364|PBP7_ECOLI|PBPG|B2134 penicillin-binding protein 7 precursor from Escherichia coli strain K12 (313 aa), FASTA scores: opt: 273, E(): 7.5e-10, (27.8% identity in 263 aa overlap); etc. Also similar to O53380|Rv3330|MTV016.30 penicillin-binding protein from Mycobacterium tuberculosis (405 aa), FASTA scores: opt: 746, E(): 1.4e-38, (47.0% identity in 266 aa overlap). Seems to contain PF00768 Peptidase_S11 domain PFAM. Belongs to peptidase family S11; also known as the D-alanyl-D-alanine carboxypeptidase 1 family. Thought to be a membrane-bound protein. Note that previously known as dacB. |
| Functional category | Cell wall and cell processes |
| Proteomics | Predicted secreted protein/surface lipoprotein - identified in culture filtrates of M. tuberculosis H37Rv; signal peptide predicted and cleavable signal sequence confirmed experimentally (See Malen et al., 2007). Identified in the culture filtrate of M. tuberculosis H37Rv using LC-MS/MS; antigen recognized by serum pool from tuberculosis patients (See Malen et al., 2008). Identified by mass spectrometry in the culture filtrate and whole cell lysates of M. tuberculosis H37Rv but not the membrane protein fraction (See de Souza et al., 2011). |
| Mutant | Non-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 3218339 | 3219214 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2911|dacB2
MRKLMTATAALCACAVTVSAGAAWADADVQPAGSVPIPDGPAQTWIVADLDSGQVLAGRDQNVAHPPASTIKVLLALVALDELDLNSTVVADVADTQAECNCVGVKPGRSYTARQLLDGLLLVSGNDAANTLAHMLGGQDVTVAKMNAKAATLGATSTHATTPSGLDGPGGSGASTAHDLVVIFRAAMANPVFAQITAEPSAMFPSDNGEQLIVNQDELLQRYPGAIGGKTGYTNAARKTFVGAAARGGRRLVIAMMYGLVKEGGPTYWDQAATLFDWGFALNPQASVGSL
Bibliography
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Malen H, Softeland T and Wiker HG [2008]. Antigen analysis of Mycobacterium tuberculosis H37Rv culture filtrate proteins. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
