ID   DLTA_STRA5              Reviewed;         511 AA.
AC   P59591;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=SAG1790;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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, ECO:0000305}.
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DR   EMBL; AE009948; AAN00653.1; -; Genomic_DNA.
DR   RefSeq; NP_688780.1; NC_004116.1.
DR   RefSeq; WP_000581010.1; NC_004116.1.
DR   AlphaFoldDB; P59591; -.
DR   SMR; P59591; -.
DR   STRING; 208435.SAG1790; -.
DR   BindingDB; P59591; -.
DR   EnsemblBacteria; AAN00653; AAN00653; SAG1790.
DR   GeneID; 66886628; -.
DR   KEGG; sag:SAG1790; -.
DR   PATRIC; fig|208435.3.peg.1797; -.
DR   HOGENOM; CLU_000022_2_12_9; -.
DR   OMA; PNIRFIR; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000000821; Chromosome.
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; IPR020845; AMP-binding_CS.
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.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..511
FT                   /note="D-alanine--D-alanyl carrier protein ligase"
FT                   /id="PRO_0000213161"
FT   BINDING         152..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         199
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         294..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         303
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         385
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         397..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         499
FT                   /ligand="D-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57416"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
SQ   SEQUENCE   511 AA;  57195 MW;  2CA784BF42D689CB CRC64;
     MIHDMIKTIE HFAETQADFP VYDILGEVHT YGQLKVDSDS LAAHIDSLGL VEKSPVLVFG
     GQEYEMLATF VALTKSGHAY IPVDQHSALD RIQAIMTVAQ PSLIISIGEF PLEVDNVPIL
     DVSQVSAIFE EKTPYEVTHS VKGDDNYYII FTSGTTGLPK GVQISHDNLL SFTNWMISDD
     EFSVPERPQM LAQPPYSFDL SVMYWAPTLA MGGTLFALPK TVVNDFKKLF ATINELPIQV
     WTSTPSFADM ALLSNDFNSE TLPQLTHFYF DGEELTVKTA QKLRQRFPKA RIVNAYGPTE
     ATVALSAVAI TDEMLETCKR LPIGYTKDDS PTYVIDEEGH KLPNGEQGEI IIAGPAVSKG
     YLNNPEKTAE AFFQFEGLPA YHTGDLGSMT DEGLLLYGGR MDFQIKFNGY RIELEDVSQN
     LNKSQYVKSA VAVPRYNKDH KVQNLLAYIV LKEGVRDDFE RDLDLTKAIK EDLKDIMMDY
     MMPSKFIYRE DLPLTPNGKI DIKGLMSEVN K