ID A0A1H9T868_9LACT Unreviewed; 505 AA.
AC A0A1H9T868;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-alanine--D-alanyl carrier protein ligase {ECO:0000256|HAMAP-Rule:MF_00593};
DE Short=DCL {ECO:0000256|HAMAP-Rule:MF_00593};
DE EC=6.2.1.54 {ECO:0000256|HAMAP-Rule:MF_00593};
DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00593};
DE AltName: Full=D-alanine-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00593};
DE Short=DAE {ECO:0000256|HAMAP-Rule:MF_00593};
GN Name=dltA {ECO:0000256|HAMAP-Rule:MF_00593};
GN ORFNames=SAMN04488559_11150 {ECO:0000313|EMBL:SER93435.1};
OS Isobaculum melis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Isobaculum.
OX NCBI_TaxID=142588 {ECO:0000313|EMBL:SER93435.1, ECO:0000313|Proteomes:UP000198948};
RN [1] {ECO:0000313|EMBL:SER93435.1, ECO:0000313|Proteomes:UP000198948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13760 {ECO:0000313|EMBL:SER93435.1,
RC ECO:0000313|Proteomes:UP000198948};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|HAMAP-Rule:MF_00593}.
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00593};
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00593}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC DltA subfamily. {ECO:0000256|HAMAP-Rule:MF_00593}.
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DR EMBL; FOHA01000011; SER93435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9T868; -.
DR STRING; 142588.SAMN04488559_11150; -.
DR OrthoDB; 9765680at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000198948; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047473; F:D-alanine [D-alanyl carrier protein] ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05945; DltA; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR HAMAP; MF_00593; DltA; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010072; DltA.
DR InterPro; IPR044507; DltA-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01734; D-ala-DACP-lig; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00593};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00593};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00593, ECO:0000313|EMBL:SER93435.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00593};
KW Reference proteome {ECO:0000313|Proteomes:UP000198948}.
FT DOMAIN 11..361
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 421..493
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 153..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 198
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 293..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 302
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 395..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 493
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
SQ SEQUENCE 505 AA; 57231 MW; CE41D60D2A1E5D8D CRC64;
MKTIIEQMND FAEMSPDTLC YDSIEKTHTY GELKWQSNQL ANAIIKKVPH LDGNMPVLIY
GEITYEMVVS FIAALKVGMF YVPVDKYTPM ERIKQIFDIA QPELIISLEA LPFEATVPVL
TLEEVQQVIE QKEVLNLPVY QTKDTDRIYA IFTSGTTGVP KGVQINHRNL LSFTDWIATD
FQVGKQKRFL CQAPFSFDLS VMDLYPALLS GGTLVPVQKQ VTDNFKKLFA YLPETKVNVW
VSTPSFMEIC LLEKTFDALH YPELTTFLFC GEELTNQTAK QLKERFPEAA IYNTYGPTEA
TVAVTQVLIT DEVLAEYPRL PIGFVKEDTQ MLIKDDEGNT LPDGEVGEMV IVGPSVSIGY
LNNEEKTAEA FYLEDGVQAY RTGDLGFLKE GLLFYQGRKD FQIKLHGYRI ELEDVDHHLE
NVSLIKAAIA VPQMKENKVA NLAAFVVAQP HTFEKEYQLT AAIKKELAES TMAYMIPQKW
IYLDELPLTA NGKIDRKTLM NEVNQ
//
