ID DLTA_STAA3 Reviewed; 485 AA. AC Q2FIE3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 104. DE RecName: Full=D-alanine--D-alanyl carrier protein ligase {ECO:0000255|HAMAP-Rule:MF_00593}; DE Short=DCL {ECO:0000255|HAMAP-Rule:MF_00593}; DE EC=6.2.1.54 {ECO:0000255|HAMAP-Rule:MF_00593}; DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00593}; DE AltName: Full=D-alanine-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00593}; DE Short=DAE {ECO:0000255|HAMAP-Rule:MF_00593}; GN Name=dltA {ECO:0000255|HAMAP-Rule:MF_00593}; GN OrderedLocusNames=SAUSA300_0835; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). 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:0000255|HAMAP-Rule:MF_00593}. CC -!- CATALYTIC ACTIVITY: CC Reaction=holo-[D-alanyl-carrier protein] + D-alanine + ATP = D-alanyl- CC [D-alanyl-carrier protein] + AMP + diphosphate; Xref=Rhea:RHEA:55132, CC Rhea:RHEA-COMP:14102, Rhea:RHEA-COMP:14103, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57416, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:138620, ChEBI:CHEBI:456215; EC=6.2.1.54; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00593}; CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00593}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00593}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC DltA subfamily. {ECO:0000255|HAMAP-Rule:MF_00593}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000255; ABD22135.1; -; Genomic_DNA. DR RefSeq; WP_000129653.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FIE3; -. DR SMR; Q2FIE3; -. DR KEGG; saa:SAUSA300_0835; -. DR HOGENOM; CLU_000022_2_12_9; -. DR OMA; VMDLYPC; -. DR UniPathway; UPA00556; -. DR Proteomes; UP000001939; Chromosome. DR AbasyAtlas; Q2FIE3; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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 FunFam; 3.30.300.30:FF:000012; D-alanine--D-alanyl carrier protein ligase; 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_dom. DR InterPro; IPR045851; AMP-b_sf. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. 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 NCBIfam; NF003417; PRK04813.1; 1. DR PANTHER; PTHR45398; -; 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; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..485 FT /note="D-alanine--D-alanyl carrier protein ligase" FT /id="PRO_1000025533" FT BINDING 144..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 189 FT /ligand="D-alanine" FT /ligand_id="ChEBI:CHEBI:57416" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 284..289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 293 FT /ligand="D-alanine" FT /ligand_id="ChEBI:CHEBI:57416" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 365 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 473 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" FT BINDING 473 FT /ligand="D-alanine" FT /ligand_id="ChEBI:CHEBI:57416" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593" SQ SEQUENCE 485 AA; 54670 MW; FFA535607F1FD328 CRC64; MTDIINKLQA FADANPQSIA VRHTTDELTY QQLMDESSKL AHRLQGSKKP MILFGHMSPY MIVGMIGAIK AGCGYVPVDT SIPEDRIKMI INKVQPEFVF NTTDESFESL EGEVFTIEDI KTSQDPVIFD SQIKDNDTVY TIFTSGSTGE PKGVQIEYAS LVQFTEWMLE LNKSGNEQQW LNQAPFSFDL SVMAIYPCLA SGGTLNLVDK NMINKPKLLN EMLTATPINI WVSTPSFMEM CLLLPTLNEE QYGSLNEFFF CGEILPHRAA KALVNRFPSA TIYNTYGPTE ATVAVTSIQI TQEILDQYPT LPVGVERPGA RLSTTDEGEL VIEGQSVSLG YLKNDQKTAE VFNFDDGIRT YHTGDKAKFE NGQWFIQGRI DFQIKLNGYR MELEEIETQL RQSEFVKEAI VVPVYKNDKV IHLIGAIVPT TEVTDNAEMT KNIKNDLKSR LPEYMIPRKF EWMEQLPLTS NGKIDRKKIA EVING //