ID A0A200JDR3_9ENTE Unreviewed; 503 AA.
AC A0A200JDR3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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=A5889_000172 {ECO:0000313|EMBL:OUZ34697.1};
OS Enterococcus sp. 9D6_DIV0238.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834192 {ECO:0000313|EMBL:OUZ34697.1, ECO:0000313|Proteomes:UP000196151};
RN [1] {ECO:0000313|EMBL:OUZ34697.1, ECO:0000313|Proteomes:UP000196151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9D6_DIV0238 {ECO:0000313|EMBL:OUZ34697.1,
RC ECO:0000313|Proteomes:UP000196151};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 9D6_DIV0238.";
RL Submitted (MAY-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUZ34697.1}.
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DR EMBL; NIBQ01000001; OUZ34697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200JDR3; -.
DR OrthoDB; 9765680at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000196151; 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; IPR020845; AMP-binding_CS.
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.
DR PROSITE; PS00455; AMP_BINDING; 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:OUZ34697.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00593};
KW Reference proteome {ECO:0000313|Proteomes:UP000196151}.
FT DOMAIN 15..357
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 413..490
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 151..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 196
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 291..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 300
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 392..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
FT BINDING 490
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00593"
SQ SEQUENCE 503 AA; 56811 MW; CCD8DF14FFEB3445 CRC64;
MITDIIEAVD RWGINEPNRP VYIEADQTYT YGELKRDSDA VAGYLQQNIE RSRPVVVYGE
LEFDMLACFL GASKAGHAYI PIEAHTPAER IEMILDVAEP ALIFSIADWP DIATQAEIIS
LEKVKEEHTI STSADTLRPV EGSQTYYIIF TSGTTGVPKG VQISHTNLLS FVNWELADFG
ISEGMRFLSQ APYSFDLSVM DLYPALVSGG SLTPMKKEII TDFKQLFKVL PTLEIEVWVS
TPSFMDICLM EPNFEQKNVK SLKIFLFCGE ELPKATAQKL LERFPDAHIF NTYGPTEATV
AISGVEITPE LLEKYDRIPI GYVKEDTHVY IMDENTELPE GEVGEIIIAG PSVSKGYMNN
KEKTEAAFFE YQGQPAYRTG DAGKLEENML IYDGRIDFQI KMHGYRIELE DIDHHLANVS
YVKQAAVVPK YHEHKVQQLV AFVVAHPNEF EKEFKLTKAI KEELGQTVMD YMIPQKFVYV
EQLPLTPNGK IDRKGLMNEV NVT
//
