DLTA_STAXY
ID DLTA_STAXY Reviewed; 487 AA.
AC Q9X2N4;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
OS Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=10085071; DOI=10.1074/jbc.274.13.8405;
RA Peschel A., Otto M., Jack R.W., Kalbacher H., Jung G., Goetz F.;
RT "Inactivation of the dlt operon in Staphylococcus aureus confers
RT sensitivity to defensins, protegrins, and other antimicrobial peptides.";
RL J. Biol. Chem. 274:8405-8410(1999).
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=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: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}.
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DR EMBL; AF032440; AAD01942.1; -; Genomic_DNA.
DR RefSeq; WP_047172670.1; NZ_PZEG01000006.1.
DR AlphaFoldDB; Q9X2N4; -.
DR SMR; Q9X2N4; -.
DR STRING; 1288.SXYLSMQ121_1843; -.
DR KEGG; sxo:SXYL_01990; -.
DR eggNOG; COG1020; Bacteria.
DR UniPathway; UPA00556; -.
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; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010072; DltA.
DR InterPro; IPR044507; DltA-like.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR TIGRFAMs; TIGR01734; D-ala-DACP-lig; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..487
FT /note="D-alanine--D-alanyl carrier protein ligase"
FT /id="PRO_0000213159"
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 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 475
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
SQ SEQUENCE 487 AA; 55729 MW; 283C975BC59E8BD2 CRC64;
MKDIIYSLIE NEKMYPEQIA IKHNTDVLTY RELNQYANKL ADLIKDTKSP LIVYGHMSPF
MIVGMIASMK AGCGYVPLDI SMPEERINTI IEKINPDFIF NTSEHSLDSN GREIVNTETL
LTDNRTVEFE SKIKDQDIAY TIFTSGSTGE PKGVQIRYES LNEFTNWMVD LNKIGENQQW
LNQAPFSFDL SVMAIYPCLA TAGTLNLVDK TMINKPKLLN DMLEQSKINV WVSTPSFMEM
CLMLPNLAET HYESLKEFFF CGEILPHKTA KMLLQRFPSA YIYNTYGPTE ATVAVTSILI
TEAVINQYNP LPVGKARPGT QLSLAENEEL IISGQCVSEG YVKDEQRSNE VFKDIDKRKS
YFTGDKATVQ DDLWFITGRI DFQVKLNGYR MELEEIEFHL RQIDVVKEAI VVPVYKNNKV
TQLQGVVVLN DLNDDKDEQT VIHDIKQELK QAMPEYMIPR KIIFKEQFPL TINGKLDRKQ
IAEDVLA
