Quick Search

Enter gene name or accession number


Search term: Rv2981c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
Imagemap from R
To navigate upstream or downstream, click on the first or last gene

General annotation
Gene nameddlA
Rv numberRv2981c
Synonym(s)ddl
TypeCDS
FunctionInvolved in cell wall formation. Along with alanine racemase, it MAKES up the D-alanine branch of the peptidoglycan biosynthetic route. [catalytic activity: ATP + D-alanine + D-alanine = ADP + phosphate + D-alanyl-D-alanine].
ProductProbable D-alanine--D-alanine ligase DdlA (D-alanylalanine synthetase) (D-ala-D-ala ligase)
CommentsRv2981c, (MTCY349.06), len: 373 aa. Probable ddlA (alternate gene name: ddl), D-alanine--D-alanine ligase a (see citation below), equivalent to Q9CBS0|Q9CBS0 D-alanine-D-alanine ligase a from Mycobacterium leprae (384 aa), FASTA scores: opt: 2001, E(): 2.4e-115, (81.75% identity in 367 aa overlap); and Q9ZGN0|DDL_MYCSM D-alanine--D-alanine ligase from Mycobacterium smegmatis (373 aa), FASTA scores: opt: 1934, E(): 3.1e-111, (77.95% identity in 372 aa overlap). Also highly similar to others e.g. Q9ZBR9|DDL_STRCO from Streptomyces coelicolor (389 aa), FASTA scores: opt: 1187, E(): 2.2e-65, (52.0% identity in 379 aa overlap); P15051|DDLA_SALTY from Salmonella typhimurium and Salmonella typhi (363 aa), FASTA scores: opt: 946, E(): 1.3e-50, (44.5% identity in 364 aa overlap); P23844|DDLA_ECOLI|DDLA|B0381|Z0477|ECS0431 from Escherichia coli strain O157:H7 and K12 (364 aa), FASTA scores: opt: 938, E(): 3.9e-50, (43.55% identity in 363 aa overlap); etc. Contains PS00843 D-alanine--D-alanine ligase signature 1. Belongs to the D-alanine--D-alanine ligase family.
Molecular mass (Da)39678.2
Isoelectric point5.1381
Gene length (bp)1122
Protein length373
Location (kb)3336.8


Functional categorycell wall and cell processes


ProteomicsIdentified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010). Identified by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Required for growth in C57BL/6J mouse spleen, by transposon site hybridization (TraSH) in H37Rv (See Sassetti and Rubin, 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


Coordinates
TypeStartEndOrientation
CDS33367963337917-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2981c|ddlA
VSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTD
ANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGP
YGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLH
RQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELEC
GVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQ
LAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLAT
MIETTLARGVGLH
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP95114
Protein Data Bank3LWB


Orthologs/Cross-references
CDC1551MT3059
Enzyme Classification6.3.2.4
Gene OntologyATP binding
cell wall
cytoplasm
cellular cell wall organization
regulation of cell shape
D-alanine-D-alanine ligase activity
peptidoglycan biosynthetic process
metal ion binding
M. bovisMb3005c
M. lepraeML1678
M. marinumMMAR_1733
M. smegmatisMSMEG_2395
UniProtP95114
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2981c


Expression Data
TBDBRv2981c


Bibliography
Feng Z, Barletta RG,
Roles of Mycobacterium smegmatis D-Alanine:D-Alanine Ligase and D-Alanine Racemase in the Mechanisms of Action of and Resistance to the Peptidoglycan Inhibitor D-Cycloserine.
Antimicrob Agents Chemother (2003) 47(1):283-91
Cited for: Gene
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
Sassetti CM, Rubin EJ,
Genetic requirements for mycobacterial survival during infection.
Proc Natl Acad Sci U S A (2003) 100(22):12989-94
Cited for: Mutant
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
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
Belanger AE, Inamine JM,
Molecular Genetics of Mycobacteria; Twelfth chapter: Genetics of Cell Wall Biosynthesis
ASM Press (2000) 1-55581-191-4:191-202
Cited for: Review