| 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 ]
|
