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Database: UniProt
Entry: Q03AZ2
LinkDB: Q03AZ2
Original site: Q03AZ2 
ID   DLTA_LACP3              Reviewed;         506 AA.
AC   Q03AZ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   20-DEC-2017, entry version 71.
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.- {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};
GN   OrderedLocusNames=LSEI_0794;
OS   Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 /
OS   KCTC 3260 / NRRL B-441).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- FUNCTION: Catalyzes the first step in the D-alanylation of
CC       lipoteichoic acid (LTA), the activation of D-alanine and its
CC       transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-
CC       dependent two-step reaction, forms a high energy D-alanyl-AMP
CC       intermediate, followed by transfer of the D-alanyl residue as a
CC       thiol ester to the phosphopantheinyl prosthetic group of the Dcp.
CC       D-alanylation of LTA plays an important role in modulating the
CC       properties of the cell wall in Gram-positive bacteria, influencing
CC       the net charge of the cell wall. {ECO:0000255|HAMAP-
CC       Rule:MF_00593}.
CC   -!- CATALYTIC ACTIVITY: D-alanine + ATP + holo-[D-alanyl-carrier
CC       protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier
CC       protein]. {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
CC       family. DltA subfamily. {ECO:0000255|HAMAP-Rule:MF_00593}.
DR   EMBL; CP000423; ABJ69630.1; -; Genomic_DNA.
DR   RefSeq; WP_011674281.1; NC_008526.1.
DR   RefSeq; YP_806072.1; NC_008526.1.
DR   ProteinModelPortal; Q03AZ2; -.
DR   SMR; Q03AZ2; -.
DR   EnsemblBacteria; ABJ69630; ABJ69630; LSEI_0794.
DR   GeneID; 4419382; -.
DR   KEGG; lca:LSEI_0794; -.
DR   PATRIC; fig|321967.11.peg.795; -.
DR   HOGENOM; HOG000229995; -.
DR   KO; K03367; -.
DR   OMA; NFYIIFT; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000001651; 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:InterPro.
DR   GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    506       D-alanine--D-alanyl carrier protein
FT                                ligase.
FT                                /FTId=PRO_1000025530.
FT   NP_BIND     152    153       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     292    297       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   NP_BIND     395    398       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     197    197       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
FT   BINDING     301    301       D-alanine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     383    383       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     494    494       ATP. {ECO:0000255|HAMAP-Rule:MF_00593}.
FT   BINDING     494    494       D-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00593}.
SQ   SEQUENCE   506 AA;  56144 MW;  2138A161D2091C71 CRC64;
     MIDNVITAID RVAAEHPTRV AYDYEGTQYT YAQLKEGSDR LAGFFAETLP EHEPIIVYGG
     QTFDMVEVFL GLSKSGHAYI PIDTHSPNER ITQVQDVAHT PAIIEVAPLP IAVPDVQIIR
     APALHEAEKT HAPISSLQHA VVGDDNYYII FTSGTTGKPK GVQISHDNLL SYVNWNISDF
     GLKEGVVAMS QPPYSFDLSV MDLYPTLVLG GTLKALPKEV TDNFKTLFAT LPKLGLNEWV
     STPSFAEIAL LDPNFNQDNY PDLTHFLFCG EELVNKTAQE LITRFPKATV YNTYGPTETT
     VAVTGMAITQ DIVDQYPRLP IGFAKPDTEI FVVDEQGNQV SAGTEGELMI VGPSVSKGYL
     NNPEKTAKAF FNVGSQRGYR SGDLATMTED GMIFYRGRTD FQVKLHGYRI ELEDVDHNLN
     QVSYIKQAST VPRYNKDHKV AQLIAFAVAK PNDFESDMKL TQAVKAELGK MVMEYMIPQR
     IIYRDKLPLT ANGKVDRKAL IAEVNH
//
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