ID   DLTC_STAA8              Reviewed;          78 AA.
AC   Q2FZW4; P0A021; Q53663;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=D-alanine--poly(phosphoribitol) ligase subunit 2;
DE            EC=6.1.1.13;
DE   AltName: Full=D-alanyl carrier protein;
DE            Short=DCP;
GN   Name=dltC; OrderedLocusNames=SAOUHSC_00871;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99185055; PubMed=10085071; DOI=10.1074/jbc.274.13.8405;
RA   Peschel A., Otto M., Jack R.W., Kalbacher H., Jung G., Goetz F.;
RT   "Inactivation of the dlt operon in Staphylococcus aureus confers
RT   sensitivity to defensins, protegrins, and other antimicrobial
RT   peptides.";
RL   J. Biol. Chem. 274:8405-8410(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC8325 genome.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of D-alanyl-lipoteichoic
CC       acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl
CC       substituent to membrane-associated LTA (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   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
CC       serine of apo-DCP (By similarity).
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
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DR   EMBL; AF101234; AAD21959.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD29996.1; -; Genomic_DNA.
DR   RefSeq; YP_499424.1; -.
DR   GeneID; 3919218; -.
DR   GenomeReviews; CP000253_GR; SAOUHSC_00871.
DR   KEGG; sao:SAOUHSC_00871; -.
DR   HOGENOM; Q2FZW4; -.
DR   OMA; Q2FZW4; EWDTPNK.
DR   BioCyc; SAUR93061:SAOUHSC_00871-MON; -.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047473; F:D-alanine-poly(phosphoribitol) ligase activity; IEA:HAMAP.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00565; -; 1.
DR   InterPro; IPR003230; D-ala_carrier.
DR   ProDom; PD015103; D-ala_carrier; 1.
DR   TIGRFAMs; TIGR01688; dltC; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Ligase; Nucleotide-binding; Phosphopantetheine.
FT   CHAIN         1     78       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 2.
FT                                /FTId=PRO_0000289881.
FT   MOD_RES      36     36       O-(pantetheine 4'-phosphoryl)serine
FT                                (Probable).
SQ   SEQUENCE   78 AA;  9063 MW;  C001D1D3D189A584 CRC64;
     MEFREQVLNL LAEVAENDIV KENPDVEIFE EGIIDSFQTV GLLLEIQNKL DIEVSIMDFD
     RDEWATPNKI VEALEELR
//