DLTA_STRMU
ID DLTA_STRMU Reviewed; 516 AA.
AC Q53526; O68576;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 4.
DT 03-AUG-2022, entry version 130.
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=SMU_1691;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RX PubMed=11029425; DOI=10.1128/jb.182.21.6055-6065.2000;
RA Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V.,
RA Neuhaus F.C., Hamilton I.R.;
RT "Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans
RT results in acid sensitivity.";
RL J. Bacteriol. 182:6055-6065(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Spatafora G.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [4]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-445.
RX PubMed=7790069; DOI=10.1128/iai.63.7.2556-2563.1995;
RA Spatafora G., Rohrer K., Barnard D., Michalek S.;
RT "A Streptococcus mutans mutant that synthesizes elevated levels of
RT intracellular polysaccharide is hypercariogenic in vivo.";
RL Infect. Immun. 63:2556-2563(1995).
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; AF051356; AAC05774.1; -; Genomic_DNA.
DR EMBL; AF050517; AAC29038.1; -; Genomic_DNA.
DR EMBL; AF049357; AAC06284.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59328.1; -; Genomic_DNA.
DR RefSeq; NP_722022.1; NC_004350.2.
DR RefSeq; WP_002262582.1; NC_004350.2.
DR AlphaFoldDB; Q53526; -.
DR SMR; Q53526; -.
DR STRING; 210007.SMU_1691; -.
DR PRIDE; Q53526; -.
DR DNASU; 1028915; -.
DR EnsemblBacteria; AAN59328; AAN59328; SMU_1691.
DR KEGG; smu:SMU_1691; -.
DR PATRIC; fig|210007.7.peg.1511; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_12_9; -.
DR OMA; VMDLYPC; -.
DR PhylomeDB; Q53526; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000002512; 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..516
FT /note="D-alanine--D-alanyl carrier protein ligase"
FT /id="PRO_0000213162"
FT BINDING 156..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 203
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 298..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 307
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 401..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT BINDING 503
FT /ligand="D-alanine"
FT /ligand_id="ChEBI:CHEBI:57416"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT CONFLICT 21..22
FT /note="AE -> EA (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="R -> A (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="T -> I (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..250
FT /note="NQLPIGVWTSTPS -> TNYHWCVDINTF (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..271
FT /note="LTH -> SNS (in Ref. 2; AAC29038 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..391
FT /note="KLRQRFPQARIVNAYGPTEATVALSALAVTDKMLETCKRLPIGYTKPDSPTF
FT IIDESGHKLANGQQGEIIVSGPAVSKGYLNNPERTAAAFFEFEGLPAYHTGDLG -> N
FT CVSVFRKQELSTLMGQQKQLLLYQLWLSLIKCLKHANVCQLAIQNQIRQPLLLMSQVIN
FT WQMVSKERLLFPVRQSLRGISIILNEQQQLSLNLKVCQLIILVIWP (in Ref. 2;
FT AAC29038 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="M -> I (in Ref. 2; AAC29038/AAC06284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57560 MW; AE9CB3C22CB54ADC CRC64;
MANKKIKDMI ATIENFAQEQ AEFPVYNILG EIHTYGELKA DSDSLAAHLD QLDLTAKSPV
VVFGGQEYAM LASFVALTKS GHAYIPIDHH SALERIEAIL EVAEPSLVIA VDDFPIDNLQ
VPVIQYSQLE EIFKQKLSYQ INHAVKGDDT YYIIFTSGTT GKPKGVQISH DNLLSFTNWM
INAEAFATPH RPQMLAQPPY SFDLSVMYWA PTLALGGTLF ALPKEITADF KQLFTTINQL
PIGVWTSTPS FVDMAMLSDD FNAQQLPHLT HFYFDGEELT VKTAKKLRQR FPQARIVNAY
GPTEATVALS ALAVTDKMLE TCKRLPIGYT KPDSPTFIID ESGHKLANGQ QGEIIVSGPA
VSKGYLNNPE RTAAAFFEFE GLPAYHTGDL GSMTDEGLLL YGGRMDFQIK FNGYRIELEE
VSQNLNKSQY IASAVAVPRY NKDHKVQNLL AYVVLKDGVE EQFERALDIT KAIKADLQDV
MMDYMMPSKF LYRKDLPLTP NGKIDIKGLM SEVNKK
