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Search term: Rv2911

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namedacB2
Rv numberRv2911
FunctionInvolved 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].
ProductProbable 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)
CommentsRv2911, (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.
Molecular mass (Da)29746.7
Isoelectric point4.8157
Gene length (bp)876
Protein length291
Location (kb)3218.34

Functional categorycell wall and cell processes

ProteomicsPredicted 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).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2911|dacB2
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 Bank2BCF

Enzyme Classification3.4.16.4
Gene Ontologyproteolysis
serine-type D-Ala-D-Ala carboxypeptidase activity
M. bovisMb2935
M. marinumMMAR_1797
M. smegmatisMSMEG_2433
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv2911

Expression Data

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
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Cited for: Proteomics
Malen H, Softeland T, Wiker HG,
Antigen analysis of Mycobacterium tuberculosis H37Rv culture filtrate proteins.
Scand J Immunol (2008) 67(3):245-52
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