A0A163PEE5 · A0A163PEE5_STAAU
- ProteinD-alanine--D-alanyl carrier protein ligase
- GenedltA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids485 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- holo-[D-alanyl-carrier protein] + D-alanine + ATP = D-alanyl-[D-alanyl-carrier protein] + AMP + diphosphate
Pathway
Cell wall biogenesis; lipoteichoic acid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 144-145 | ATP (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 189 | D-alanine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 284-289 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NTYGPT | ||||||
Binding site | 293 | D-alanine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 365 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 473 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 473 | D-alanine (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | D-alanine [D-alanyl carrier protein] ligase activity | |
Biological Process | lipoteichoic acid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-alanine--D-alanyl carrier protein ligase
- EC number
- Short namesDCL
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A163PEE5
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-342 | AMP-dependent synthetase/ligase | ||||
Sequence: QAFADANPQSIAVRHTTDELTYQQLMDESSKLAHRLQGSKKPMILFGHMSPYMIVGMIGAIKAGCGYVPVDTSIPEDRIKMIINKVQPEFVFNTTDESFESLAGEVFTIEDIKTSQDPVIFDSQIKDNDTVYTIFTSGSTGEPKGVQIEYASLVQFTEWMLELNKSGNEQQWLNQAPFSFDLSVMAIYPCLASGGTLNLVDKNMINKPKLLNEMLTATPINIWVSTPSFMEMCLLLPTLNEEQYGSLNEFFFCGEILPHRAAKALVSRFPSATIYNTYGPTEATVAVTSIQITQEILDQYPTLPVGVERPGARLSTTDEGELVIEGQSVSLGYL | ||||||
Domain | 395-473 | AMP-binding enzyme C-terminal | ||||
Sequence: EIETQLRQSEFVKEAIVVPVYKNDKVIHLIGAIVPTTEVTDNAEMTKNIKNDLKSRLPEYMIPRKFEWMEQLPLTSNGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length485
- Mass (Da)54,585
- Last updated2016-07-06 v1
- Checksum8F44ECA752ECF633
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAFMT010000029 EMBL· GenBank· DDBJ | NDR17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UAUX01000004 EMBL· GenBank· DDBJ | SPZ97222.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UELG01000004 EMBL· GenBank· DDBJ | SRZ65215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UHAI01000002 EMBL· GenBank· DDBJ | SUK17162.1 EMBL· GenBank· DDBJ | Genomic DNA |