ID   DLTA_STRP2              Reviewed;         516 AA.
AC   Q04HZ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=D-alanine--poly(phosphoribitol) ligase subunit 1;
DE            EC=6.1.1.13;
DE   AltName: Full=D-alanine-activating enzyme;
DE            Short=DAE;
DE   AltName: Full=D-alanine-D-alanyl carrier protein ligase;
DE            Short=DCL;
GN   Name=dltA; OrderedLocusNames=SPD_2005;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17041037; DOI=10.1128/JB.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M.,
RA   Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of
RT   Streptococcus pneumoniae and comparison with that of unencapsulated
RT   laboratory strain R6.";
RL   J. Bacteriol. 189:38-51(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of D-alanyl-lipoteichoic
CC       acid (LTA). Catalyzes an ATP-dependent two-step reaction where it
CC       forms a high energy D-alanyl AMP intermediate and transfers the
CC       alanyl residues from AMP to Dcp (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + D-alanine + poly(ribitol phosphate) =
CC       AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. DltA subfamily.
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DR   EMBL; CP000410; ABJ54767.1; -; Genomic_DNA.
DR   RefSeq; YP_817391.1; -.
DR   GeneID; 4442941; -.
DR   GenomeReviews; CP000410_GR; SPD_2005.
DR   KEGG; spd:SPD_2005; -.
DR   OMA; Q04HZ7; AFFEFEG.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047473; F:D-alanine-poly(phosphoribitol) ligase activity; IEA:EC.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00593; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR010072; D_ala_DACP_lig.
DR   PANTHER; PTHR11968:SF34; D_ala_DACP_lig; 1.
DR   Pfam; PF00501; AMP-binding; 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.
FT   CHAIN         1    516       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_1000025536.
SQ   SEQUENCE   516 AA;  57427 MW;  C20C9E7F8EB7150B CRC64;
     MSNKPIADMI ETIEHFAQTQ PSYPVYNVLG QEHTYGDLKA DSDSLAAVID QLGLPEKSPV
     VVFGGQEYEM LATFVALTKS GHAYIPIDSH SALERVSAIL EVAEPSLIIA ISAFPLEQVS
     TPMINLAQVQ EAFAQGNNYE ITHPVKGDDN YYIIFTSGTT GKPKGVQISH DNLLSFTNWM
     ITDKEFATPS RPQMLAQPPY SFDLSVMYWA PTLALGGTLF TLPSVITQDF KQLFAAIFSL
     PIAIWTSTPS FADMAMLSEY FNSEKMPGIT HFYFDGEELT VKTAQKLRER FPNARIINAY
     GPTEATVALS AVAVTDEMLA TLKRLPIGYT KADSPTFIID EEGNKLPNGE QGEIIVSGPA
     VSKGYMNNPE KTAEAFFEFE DLPAYHTGDV GTMTDEGLLL YGGRMDFQIK FNGYRIELED
     VSQNLNKSRF IESAVAVPRY NKDHKVQNLL AYVILKDGVR EQFERDIDIT KAIKEDLTDI
     MMSYMMPSKF LYRDSLPLTP NGKIDIKGLI NEVNKR
//