DLTA_LACRH
ID DLTA_LACRH Reviewed; 506 AA.
AC P35854;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; Synonyms=dae;
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21.
RC STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC / NCIMB 6375 / NCTC 12953;
RX PubMed=1385594; DOI=10.1128/jb.174.14.4707-4717.1992;
RA Heaton M.P., Neuhaus F.C.;
RT "Biosynthesis of D-alanyl-lipoteichoic acid: cloning, nucleotide sequence,
RT and expression of the Lactobacillus casei gene for the D-alanine-activating
RT enzyme.";
RL J. Bacteriol. 174:4707-4717(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC / NCIMB 6375 / NCTC 12953;
RA Debabov D.V., Heaton M.P., Zhang Q., Stewart K., Lambalot R.H.,
RA Neuhaus F.C.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC / NCIMB 6375 / NCTC 12953;
RX PubMed=10781555; DOI=10.1128/jb.182.10.2855-2864.2000;
RA Debabov D.V., Kiriukhin M.Y., Neuhaus F.C.;
RT "Biosynthesis of lipoteichoic acid in Lactobacillus rhamnosus: role of DltD
RT in D-alanylation.";
RL J. Bacteriol. 182:2855-2864(2000).
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 ECO:0000305}.
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; M83993; AAA25234.1; -; Genomic_DNA.
DR EMBL; U43894; AAB17657.1; -; Genomic_DNA.
DR EMBL; AF192553; AAF09201.1; -; Genomic_DNA.
DR RefSeq; WP_015764309.1; NZ_WPCQ01000011.1.
DR AlphaFoldDB; P35854; -.
DR SMR; P35854; -.
DR STRING; 568703.LGG_00777; -.
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; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding.
FT CHAIN 1..506
FT /note="D-alanine--D-alanyl carrier protein ligase"
FT /id="PRO_0000213145"
FT BINDING 152..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 197
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 292..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 301
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 395..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 494
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
SQ SEQUENCE 506 AA; 55867 MW; 6185201898153961 CRC64;
MIDNVITAID RVAAEHPTRV AYDYEGTQYT YAQLKEGSDR LAGFFAESLP AGEPIIVYGG
QTFDMVEVFL GLSKSGHAYI PIDTHSPNER ITQVQDVAHA PAVIEVAPLP ITVPDVKIIR
APALHQAEQS HAPIHSLQHA VAGDDNYYII FTSGTTGKPK GVQISHDNLL SYVNWNISDF
GLEEGVVAMS QPPYSFDLSV MDLYPTLVLG GTLKALPKEV TDNFKELFAT LPKLGLNEWV
STPSFVEIAL LDPNFKQENY PNLTHFLFCG EELVNKTAQA LITRFPKATV YNTYGPTEAT
VAVTGMAITQ AIVDQYPRLP IGYAKPDTNV YVVDEQGEQV SAGTEGELMI VGPSVSKGYL
NNPDKTAAAF FKAGNQRGYR SGDLVTMTAD GMVFYRGRTD FQVKLHGYRI ELEDVDHNLN
QVSYIKQAST VPRYDKDHKV AQLIAFAVAK PNDFDSEMKL TQAIKAELGK MVMEYMIPQR
IIYRDQLPLT ANGKVDRKAL IAEVNH
