AC   MF_00593;
DC   Protein; auto
TR   HAMAP; MF_00593; -; 1; level=0
XX
Names: DltA
XX
ID   DLTA
DE   RecName: Full=D-alanine--D-alanyl carrier protein ligase;
DE            Short=DCL;
DE            EC=6.2.1.54;
DE   AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1;
DE   AltName: Full=D-alanine-activating enzyme;
DE            Short=DAE;
GN   Name=dltA;
XX
CC   -!- FUNCTION: Catalyzes the first step in the D-alanylation of lipoteichoic
CC       acid (LTA), the activation of D-alanine and its transfer onto the D-
CC       alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step
CC       reaction, forms a high energy D-alanyl-AMP intermediate, followed by
CC       transfer of the D-alanyl residue as a thiol ester to the
CC       phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA
CC       plays an important role in modulating the properties of the cell wall
CC       in Gram-positive bacteria, influencing the net charge of the cell wall.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-alanine + holo-[D-alanyl-carrier protein] = AMP + D-
CC         alanyl-[D-alanyl-carrier protein] + diphosphate;
CC         Xref=Rhea:RHEA:55132, Rhea:RHEA-COMP:14102, Rhea:RHEA-COMP:14103,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138620, ChEBI:CHEBI:456215;
CC         EC=6.2.1.54;
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       DltA subfamily.
XX
DR   Pfam; PF00501; AMP-binding; 1; trigger=no
DR   Pfam; PF13193; AMP-binding_C; 1; trigger=no
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1; trigger=no
DR   NCBIfam; TIGR01734; D-ala-DACP-lig; 1; trigger=no
DR   PROSITE; PS00455; AMP_BINDING; 1; trigger=no
XX
KW   ATP-binding
KW   Cytoplasm
KW   Ligase
KW   Nucleotide-binding
XX
GO   GO:0047473; F:D-alanine [D-alanyl carrier protein] ligase activity
GO   GO:0005737; C:cytoplasm
GO   GO:0070395; P:lipoteichoic acid biosynthetic process
XX
FT   From: DLTA_BACCR (Q81G39)
FT   BINDING         152..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T-S
FT   BINDING         292..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N-[TA]-Y-G-P-T
FT   BINDING         394..397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: Y-x-G-R
FT   BINDING         197
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT   Condition: D
FT   BINDING         301
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT   Condition: V
FT   BINDING         383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         492
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT   Condition: K
FT   BINDING         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 485-516;
Related: None;
Template: P39581; Q81G39; Q99ZA6;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.33 2023/06/01
//