BSGatlas

dltA

BSGatlas-gene-4477

BSGatlas

Description	Information
Coordinates	3952275..3953786
Genomic Size	1512 bp
Name	dltA
Outside Links	SubtiWiki
	BsubCyc
Strand	+
Type	CDS

SubtiWiki

Description	Information
Alternative Name	dae
	dltA
	dltA
	ipa-5r
Category	SW 1 Cellular processes
	SW 1.1 Cell envelope and cell division
	SW 1.1.1 Cell wall synthesis
	SW 1.1.1.4 Biosynthesis of teichoic acid
	SW 2 Metabolism
	SW 2.6 Additional metabolic pathways
	SW 2.6.1 Biosynthesis of cell wall components
	SW 2.6.1.3 Biosynthesis of teichoic acid
	SW 4 Lifestyles
	SW 4.3 Coping with stress
	SW 4.3.2 Cell envelope stress proteins (controlled by SigM, V, W, X, Y)
Description	D-alanyl-D-alanine carrier protein ligase, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides
Enzyme Classifications	EC 6.1.1.13: D-alanine-poly(phosphoribitol) ligase
Function	biosynthesis of teichoic acid
Is essential?	no
Isoelectric point	4.93
Locus Tag	BSU_38500
Molecular weight	55.6412
Name	dltA
Product	D-alanyl-D-alanine carrier protein ligase

RefSeq

Description	Information
Alternative Locus Tag	BSU38500
Description	Evidence 1a: Function from experimental evidencesin the studied strain; PubMedId: 7797557, 11222605,14665680, 15955059, 18847223, 19324056, 23858088; Producttype e: enzyme
Enzyme Classifications	EC 6.1.1.13: D-alanine-poly(phosphoribitol) ligase
Functions	16.13: Shape
	16.2: Construct biomass (Anabolism)
	16.8: Protect
Locus Tag	BSU_38500
Name	dltA
Title	D-alanine:D-alanyl-carrier protein ligasesubunit
Type	CDS

BsubCyc

Description	Information
Alternative Name	dae
	ipa-5r
Citation	Abe T;Hashimoto Y;Zhuang Y;Ge Y;Kumano T;Kobayashi M Peptide Bond Synthesis by a Mechanism Involving an Enzymatic Reaction and a Subsequent Chemical Reaction. J Biol Chem 291(4);1735-50 (2016) PUBMED: 26586916
	Guariglia-Oropeza V;Helmann JD Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids. J Bacteriol 193(22);6223-32 (2011) PUBMED: 21926231
	Ho TD;Hastie JL;Intile PJ;Ellermeier CD The Bacillus subtilis extracytoplasmic function σ factor σ(V) is induced by lysozyme and provides resistance to lysozyme. J Bacteriol 193(22);6215-22 (2011) PUBMED: 21856855
	Kiriukhin MY;Neuhaus FC D-alanylation of lipoteichoic acid: role of the D-alanyl carrier protein in acylation. J Bacteriol 183(6);2051-8 (2001) PUBMED: 11222605
	Neuhaus FC;Baddiley J A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev 67(4);686-723 (2003) PUBMED: 14665680
Comment	General Background Wall teichoic acids, as well as type I and IV lipoteichoic acids, are modified with \|FRAME: D-ALANINE\| residues, and the enzymes required for this process are encoded by the dltABCD operon \|CITS: [1385594]\|. The process starts in the cytoplasm, where \|FRAME: EC-6.2.1.M5\| (DltA) activates \|FRAME: D-ALANINE\| using ATP to form a high-energy \|FRAME: CPD-19306\| intermediate and subsequently transfers it to the phosphopantheinyl prosthetic group of the \|FRAME: D-alanine-carrier-protein\| (DltC) \|CITS: [18847223][18784082][19324056]\|. The product of the DltD gene contains a single putative N-terminal transmembrane helix and a large globular domain. While the exact activity of the enzyme is still not well understood, the gene was cloned and sequenced from \|FRAME: TAX-1582\|, and a mutant was constructed by insertional mutagenesis. The mutant lost the ability to incorporate D-alanine into lipoteichoic acids, a defect that could be complemented by the expression of an intact version of the gene \|CITS: [10781555]\|. The protein was shown to bind to DltC and to possess a thioesterase activity, and thus it was suggested that it may catalyze the final D-alanyl transfer from DltC to teichoic acid. However this could not be demonstrated in vitro \|CITS: [10781555]\|. The discovery of substantial amounts of \|FRAME: 1-Phosphatidyl-2-O-D-Ala-Glycerol\| in lipid lysate from \|FRAME: TAX-1423\| \|CITS: [26998233]\| has led to a new hypothesis. According to this hypothesis, DltD may catalyze the transfer of DltC-bound D-alanyl group to \|FRAME: L-1-PHOSPHATIDYL-GLYCEROL phosphatidylglycerol\| in the bacterial membrane by a thermodynamically spontaneous esterification reaction. \|FRAME: 1-Phosphatidyl-2-O-D-Ala-Glycerol\| in turn may serve as the lipid intermediate for subsequent D-alanylation of teichoic acids, catalyzed by DltB \|CITS: [27134729]\|. About This enzyme The dlt operon of \|FRAME: TAX-224308\| was discovered based on its similarity to the genes from \|FRAME: TAX-1582\| \|CITS: [7797557]\|. Each of the four genes was inactivated, and analysis of the mutants confirmed that they lacked \|FRAME: D-ALANINE\| in both their lipoteichoic acids and their wall teichoic acids \|CITS: [7797557]\|. The \|FRAME: BSU38500\| and \|FRAME: BSU38520\| genes of \|FRAME: TAX-224308\| were cloned with a C-terminal His₆ tag and expressed in \|FRAME: TAX-562\|, and the recombinant proteins were purified to homogeneity \|CITS: [15955059]\|. The apo DltC protein was efficiently modified to a holo form by both AcpS (the PPTase of primary metabolism) and Sfp (the PPTase of secondary metabolism). The purified DltA protein activated only \|FRAME: D-ALANINE\|, and was rather specific for the D-alanyl-carrier protein (it has some activity with the fatty acid ACP, but the Km for that substrate is in the mM range) \|CITS: [15955059]\|. A crystal structure at 2.0 Å resolution has been reported for the DltA protein from \|FRAME: TAX-1396\| in complex with the \|FRAME: CPD-19306\| intermediate \|CITS: [18847223]\|.
Description	D-alanine--[D-alanyl carrier protein] ligase
Gene Ontology	GO:0000166 nucleotide binding
	GO:0003824 catalytic activity
	GO:0005524 ATP binding
	GO:0005737 cytoplasm
	GO:0008152 metabolic process
	GO:0016208 AMP binding
	GO:0016874 ligase activity
	GO:0019350 teichoic acid biosynthetic process
	GO:0047473 D-alanine [D-alanyl carrier protein] ligase activity
	GO:0070395 lipoteichoic acid biosynthetic process
Locus Tag	BSU38500
Molecular weight	55.809
Name	dltA

Nicolas et al. predictions

Description	Information
Expression neg. correlated with	BSU23450, new_1255943_1256078, BSU23460, new_1211286_1211370, BSU23470, new_1565737_1565848, new_3072180_3072285, new_2119268_2119353, BSU09889, BSU14320
Expression pos. correlated with	BSU38510, BSU38530, BSU38520, new_3956402_3956491, BSU38499, BSU38540, BSU30540, BSU00150, BSU07260, BSU28010
Highly expressed condition	(C30) Cellsgrown overnight on LB agar plates at 30°Cwere harvested and used to inoculate pre-warmed minimal medium at OD600 of 0.5 (D. Dubnau, R. Davidoff-Abelson, J Mol Biol 56, 209, Mar 14, 1971). After growth at 37°C with vigorous shaking, cells were diluted ten times in fresh pre-warmed minimal medium and samples were harvested after a period of 30 minutes [C30] , i.e. before maximal induction of competence, and after a period of 90 minutes [C90], i.e. when competence induction was maximal.
	(Cold) Cells were grown in a synthetic medium (J. Stülke, R. Hanschke, M. Hecker, J Gen Microbiol 139, 2041, Sep, 1993) with 0.2 % glucose as carbon source (Belitsky Minimal Medium/BMM) at 37 °C with vigorous shaking. Stress was applied to exponentially growing cultures at OD500nm of 0.4. Samples were harvested before stress [BMM]; after a rapid temperature up-shift from 37 °C to 48 °C [Heat]; after a temperature down-shift from 37 °C to 18 °C [Cold]. Ethanol stress was imposed by adding ethanol to a final concentration of 4 % (v/v) and cells were harvested 10 minutes after ethanol addition [Etha].
	(dia0) Diamide was added to an exponentially growing culture (OD600 approx. 0.6) at a sub-lethal concentration(0.5 mM) and growth continued at 37°C with vigorous shaking. Samples were collected 0, 5 and 15 minutes after diamide addition [dia0, dia5 and dia15].
	(G150) Purified spores were obtained by growing cells in DSM medium (P. Schaeffer, J. Millet, J. P. Aubert, Proc Natl Acad Sci U S A 54, 704, Sep, 1965) at 37°C for 48 hours after which they were washed ten times in ice cold distilled waterover a period of 5 days. Purified spores were heat activated at 70°C in Tris 10 mM pH8.4 and germination was initiated by the addition of L-alanine 10 mM (A. Moir, J Bacteriol 146, 1106, Jun, 1981). After incubation for one hour at 37°C, the culture was diluted with an equal volume of 2X LBmedium and germinating cells were harvested at 135, 150 or 180 minutes after addition of L-alanine [G135, G150 and G180].
	(H2O2) Cells were grown in LB medium at 37°C. At OD540 of 0.3, the culture were divided into four subcultures and diamide 0.6 mM [Diami], paraquat 0.4 mM [Paraq], H2O2 0.1mM [H2O2] or no oxidative drug [Oxctl] were added to the medium. Samples were taken 10 minutes after addition
	(LBexp) Cells were grown in Luria-Bertani medium (Sigma) [LB] at 37°C with vigorous shaking in flasks. Overnight cultures were diluted 2000-fold in fresh pre-warmed medium and samples were collected during the exponential [exp], transition [tran] and stationary [stat] phases of the growth cycle .
	(LBGexp) Cells were grown in Luria-Bertani medium (Sigma) supplemented with glucose 0.3 % [LBG] at 37°C with vigorous shaking in flasks. Overnight cultures were diluted 2000-fold in fresh pre-warmed medium and samples were collected during the exponential [exp], transition [tran] and stationary [stat] phases of the growth cycle .
	(LPh) Cells were harvested (i) during exponential growth in high phosphate defined medium [HPh]; (ii) during exponential growth in low phosphate defined medium [LPh] (J. P. Muller, Z. An, T. Merad, I. C. Hancock, C. R. Harwood, Microbiology 143, 947, Mar, 1997);and (iii) at three hours after the outset of the phosphate-limitation induced stationary phase [LPhT].
	(Oxctl) Cells were grown in LB medium at 37°C. At OD540 of 0.3, the culture were divided into four subcultures and diamide 0.6 mM [Diami], paraquat 0.4 mM [Paraq], H2O2 0.1mM [H2O2] or no oxidative drug [Oxctl] were added to the medium. Samples were taken 10 minutes after addition
	(Paraq) Cells were grown in LB medium at 37°C. At OD540 of 0.3, the culture were divided into four subcultures and diamide 0.6 mM [Diami], paraquat 0.4 mM [Paraq], H2O2 0.1mM [H2O2] or no oxidative drug [Oxctl] were added to the medium. Samples were taken 10 minutes after addition
Lowely expressed condition	(BC) Cultures were inoculated from frozen glycerol stocks and grown overnight in LB at 37°C. These cultures were thendiluted, plated onto LB plates, and incubated for 16 h at 37°C. Cells were harvested from plates containing individual colonies [BI] andfrom plates with confluen growth [BC].
	(HiOs) Cells were grown in Spizizen’s minimal medium (SMM) (C. Anagnostopoulos, J. Spizizen, J Bacteriol 81, 741, May, 1961) with vigorous agitation. The control culture was grown at 37 °C [SMMPr]. For growth at high or low temperatures, pre-cultures were grown at 37 °C, diluted to an OD578nm of 0.1 and subsequently transferred to 51 °C [HiTm] and 16 °C [LoTm], respectively. For the growth at high salinity, the salinity of the medium was adjusted by adding NaCl (5 M stock solution) to produce a final concentration of 1.2 M [HiOs].
	(M9stat) Cells were grown in M9 supplemented with glucose (0.3 %) at 37°C with vigorous shaking. The composition of the M9 minimal medium is (per liter): 8.5 g Na2HPO4.2H20, 3 g KH2PO4, 1 g NH4Cl and 0.5 g NaCl. The following solutions were individually sterilized and added (volumes per liter of medium): 1 ml 0.1 M CaCl2.2H2O, 1 ml 1 M MgSO4.7H2O, 1 ml 50 mM Fe-Citrate. Also added was 10 ml of a trace salts solution containing (per liter): 170 mg ZnCl2, 100 mg MnCl2.4H2O, 60 mg CoCl2.6H2O, 60 mg Na2MoO4.2H2O and 43 mg CuCl2.2H2O. Overnight cultures were diluted 2000-fold in pre-warmed M9 medium and samples were harvested during exponential growth [M9exp], at the transition phase [M9tran] and during stationary phase [M9stat].
	(S2) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S3) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S4) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S5) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S6) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S7) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
	(S8) Cells were grown in CH medium at 37°C and sporulation was induced by resuspension in warm sporulation medium as described by Sterlini and Mandelstam (J. M. Sterlini, J. Mandelstam, Biochem J 113, 29, Jun, 1969). The initiation of sporulation was designated T0, the time of resuspension. Samples were harvested at hourly intervals for 6 hours [S0 to S6] for the first set of experiments and for 8 hours [S0 to S8] for a second set of experiments.
Name	dltA

KEGG Pathways

Description	Information
Pathway	D-Alanine metabolism (ko00473)
	Metabolic pathways (ko01100)
	Cationic antimicrobial peptide (CAMP) resistance (ko01503)
	Two-component system (ko02020)

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