ID   DLTA_STAA3              Reviewed;         485 AA.
AC   Q2FIE3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=SAUSA300_0835;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD22135.1; -; Genomic_DNA.
DR   RefSeq; YP_493535.1; -.
DR   GeneID; 3913697; -.
DR   GenomeReviews; CP000255_GR; SAUSA300_0835.
DR   KEGG; saa:SAUSA300_0835; -.
DR   HOGENOM; Q2FIE3; -.
DR   OMA; Q2FIE3; CVKSGHA.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    485       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_1000025533.
SQ   SEQUENCE   485 AA;  54670 MW;  FFA535607F1FD328 CRC64;
     MTDIINKLQA FADANPQSIA VRHTTDELTY QQLMDESSKL AHRLQGSKKP MILFGHMSPY
     MIVGMIGAIK AGCGYVPVDT SIPEDRIKMI INKVQPEFVF NTTDESFESL EGEVFTIEDI
     KTSQDPVIFD SQIKDNDTVY TIFTSGSTGE PKGVQIEYAS LVQFTEWMLE LNKSGNEQQW
     LNQAPFSFDL SVMAIYPCLA SGGTLNLVDK NMINKPKLLN EMLTATPINI WVSTPSFMEM
     CLLLPTLNEE QYGSLNEFFF CGEILPHRAA KALVNRFPSA TIYNTYGPTE ATVAVTSIQI
     TQEILDQYPT LPVGVERPGA RLSTTDEGEL VIEGQSVSLG YLKNDQKTAE VFNFDDGIRT
     YHTGDKAKFE NGQWFIQGRI DFQIKLNGYR MELEEIETQL RQSEFVKEAI VVPVYKNDKV
     IHLIGAIVPT TEVTDNAEMT KNIKNDLKSR LPEYMIPRKF EWMEQLPLTS NGKIDRKKIA
     EVING
//