ID   DLTA_STRPM              Reviewed;         512 AA.
AC   Q48SZ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=M28_Spy1054;
OS   Streptococcus pyogenes serotype M28.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=319700;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS6180 / Serotype M28;
RX   PubMed=16088825; DOI=10.1086/430618;
RA   Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D.,
RA   Beres S.B., Lefebvre R.B., Musser J.M.;
RT   "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT   potential new insights into puerperal sepsis and bacterial disease
RT   specificity.";
RL   J. Infect. Dis. 192:760-770(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; CP000056; AAX72167.1; -; Genomic_DNA.
DR   RefSeq; YP_280522.1; -.
DR   GeneID; 3573784; -.
DR   GenomeReviews; CP000056_GR; M28_Spy1054.
DR   KEGG; spb:M28_Spy1054; -.
DR   HOGENOM; Q48SZ3; -.
DR   OMA; Q48SZ3; AFFEFEG.
DR   BioCyc; SPYO319701:M28_SPY1054-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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    512       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 1.
FT                                /FTId=PRO_1000025541.
SQ   SEQUENCE   512 AA;  56952 MW;  54081167556BBE51 CRC64;
     MIKDMIDSIE QFAQTQADFP VYDCLGEHRT YGQLKRDSDS IAAFIDSLAL LAKSPVLVFG
     AQTYDMLATF VALTKSGHAY IPVDVHSAPE RILAIIEIAK PSLIIAIEEF PLTIEGISLV
     SLSEIESAKL AEMPYERTHS VKGDDNYYII FTSGTTGQPK GVQISHDNLL SFTNWMIEDA
     AFDVPKQPQM LAQPPYSFDL SVMYWAPTLA LGGTLFALPK ELVADFKQLF TTIAQLPVGI
     WTSTPSFADM AMLSDDFCQA KMPALTHFYF DGEELTVSTA RKLFERFPSA KIINAYGPTE
     ATVALSAIEI TREMVDNYTR LPIGYPKPDS PTYIIDEDGK ELASGEQGEI IVTGPAVSKG
     YLNNPEKTAE AFFTFKGQPA YHTGDIGSLT EDNILLYGGR LDFQIKYAGY RIELEDVSQQ
     LNQSPMVASA VAVPRYNKEH KVQNLLAYIV VKDGVKERFD RELELTKAIK ASVKDHMMSY
     MMPSKFLYRD SLPLTPNGKI DIKTLINEVN NR
//