(data stored in ACNUC9435 zone)

SWISSPROT: DLTA_LISIN

ID   DLTA_LISIN              Reviewed;         510 AA.
AC   Q92D47;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, 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=lin0973;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
DR   EMBL; AL596167; CAC96204.1; -; Genomic_DNA.
DR   PIR; AD1554; AD1554.
DR   RefSeq; WP_010990699.1; NC_003212.1.
DR   SMR; Q92D47; -.
DR   STRING; 272626.lin0973; -.
DR   EnsemblBacteria; CAC96204; CAC96204; CAC96204.
DR   KEGG; lin:dltA; -.
DR   eggNOG; ENOG4108IQD; Bacteria.
DR   eggNOG; COG1020; LUCA.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; MDLYPCL; -.
DR   OrthoDB; 377638at2; -.
DR   BioCyc; GCF_000195795:LIN_RS04970-MONOMER; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000002513; 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   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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   InterPro; IPR010072; DltA.
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;
DR   PRODOM; Q92D47.
DR   SWISS-2DPAGE; Q92D47.
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..510
FT                   /note="D-alanine--D-alanyl carrier protein ligase"
FT                   /id="PRO_0000213146"
FT   NP_BIND         157..158
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   NP_BIND         297..302
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         202
FT                   /note="D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         306
FT                   /note="D-alanine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         389
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         498
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
FT   BINDING         498
FT                   /note="D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00593"
SQ   SEQUENCE   510 AA;  57742 MW;  5BB5E40208723147 CRC64;
     MTTSIIERID AWAEKTPDFP CYEYAGTRLS YKELKRQSDA FGSFLLNTLN SDKEKPIIVY
     GHMSPLMLIA FLGTIKSGRA YVPVDVSMPV ERIEQIKKAA DPALFICTEE LPSNLTITGC
     PVLTQDQLMD ALEKHFEEVP DPAECVKNDD NYYIIYTSGS TGNPKGVQIS QNNLVSFSNW
     ILQDFSLRQG LRFLNQAPFS FDLSVMDLYP SLLSGGTLVP LDKTITANMK DLYREIPAQN
     FDVWVSTPSF ADLCLLDDNF NQENNPNLTR FLFCGEVLAK KTASELLDRF PDAVIYNTYG
     PTEATVAVTQ VKVTRELIDA YPSLPLGVIK PDMRLHIVDQ ETGEILPEGE KGEIILIGAS
     VSKGYLNEPE KTDQVFFDYK GYQAYHTGDS GVIKDGYLFF QGRLDFQIKL HGYRIELEDI
     ENNLKKVSYI QNCAIIPKMK DEKVDMLVAQ VIPSSHDFEK EYQLSAAIKN ELKEFMPAYM
     IPRKWIYKTE FPLTMNGKID RKALNSEVNK
//

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