ID   DLTA_STAHJ              Reviewed;         485 AA.
AC   Q4L4U5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=SH2021;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05330.1; -; Genomic_DNA.
DR   RefSeq; YP_253936.1; -.
DR   GeneID; 3482302; -.
DR   GenomeReviews; AP006716_GR; SH2021.
DR   KEGG; sha:SH2021; -.
DR   NMPDR; fig|279808.3.peg.2392; -.
DR   HOGENOM; Q4L4U5; -.
DR   OMA; Q4L4U5; THIKHEL.
DR   BioCyc; SHAE279808:SH2021-MON; -.
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_0000213158.
SQ   SEQUENCE   485 AA;  54705 MW;  6724289A0688ABB3 CRC64;
     MTDIINLIND FGQSNPERVA VRHKDEELTY QQLMDESSKL AHLLQDNHKP LIVYGHMSPY
     MLVGMIGAIK AGCGYVPIDT SVPSERVNMI INKVQPDIIF NTSDTQLNHS NIQELTIQSI
     QDSDNPTLFD SQMGLTDVVY TIFTSGSTGE PKGVQIEYAS LIEFAEWMVS LNESEGSQEW
     LNQAPFSFDL SVMAIYPCLT SGGTLNLVDK EMINKPKLLN EMLVNTPINA WVSTPSFMEM
     CLLLPNLNES SYPSLNHFFF CGEILPHRTA KALLDRYPSA VVYNTYGPTE ATVAVTGIKL
     TPEVIEAYNP LPVGVSRPNT SLFTTDEGEL VIKGNSVSLG YLDNKEKTDA VFNFEDGLRI
     YHTGDKAIEK DGQWFIQGRI DFQIKLNGYR MELEEIETQL RQSEFVRETV VVPVYKNNKV
     IHLIGAVVPT EEVRDDLEMT RQIKSELKSR LPEYMIPRKF VWMKQLPLTS NGKLDRKQVA
     EDINA
//