Identification |
HMDB Protein ID
| HMDBP13868 |
Secondary Accession Numbers
| None |
Name
| D-alanine--D-alanyl carrier protein ligase |
Synonyms
|
- DCL
- D-alanine--poly(phosphoribitol) ligase subunit 1
- D-alanine-activating enzyme
- DAE
|
Gene Name
| DLTA |
Protein Type
| Unknown |
Biological Properties |
General Function
| Not Available |
Specific Function
| Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. |
Pathways
|
- Cationic antimicrobial peptide (CAMP) resistance
- D-Amino acid metabolism
- lipoteichoic acid biosynthesis
- Two-component system
|
Reactions
| Not Available |
GO Classification
|
Biological Process |
lipoteichoic acid biosynthetic process |
Cellular Component |
cytoplasm |
Molecular Function |
ATP binding |
D-alanine [D-alanyl carrier protein] ligase activity |
|
Cellular Location
|
Not Available
|
Gene Properties |
Chromosome Location
| Not Available |
Locus
| Not Available |
SNPs
| Not Available |
Gene Sequence
|
Not Available
|
Protein Properties |
Number of Residues
| 485 |
Molecular Weight
| 54704.98 |
Theoretical pI
| 4.944 |
Pfam Domain Function
|
|
Signals
|
Not Available
|
Transmembrane Regions
|
Not Available
|
Protein Sequence
|
Not Available
|
External Links |
GenBank ID Protein
| Not Available |
UniProtKB/Swiss-Prot ID
| Q4L4U5 |
UniProtKB/Swiss-Prot Entry Name
| DLTA_STAHJ |
PDB IDs
|
Not Available |
GenBank Gene ID
| Not Available |
GeneCard ID
| Not Available |
GenAtlas ID
| Not Available |
HGNC ID
| Not Available |
References |
General References
| - Takeuchi F, Watanabe S, Baba T, Yuzawa H, Ito T, Morimoto Y, Kuroda M, Cui L, Takahashi M, Ankai A, Baba S, Fukui S, Lee JC, Hiramatsu K: Whole-genome sequencing of staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species. J Bacteriol. 2005 Nov;187(21):7292-308. doi: 10.1128/JB.187.21.7292-7308.2005. [PubMed:16237012 ]
|