ID   DLTC_LACDB              Reviewed;          80 AA.
AC   Q047K9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=LBUL_1983;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000412; ABJ59363.1; -; Genomic_DNA.
DR   RefSeq; YP_813801.1; -.
DR   GeneID; 4434733; -.
DR   GenomeReviews; CP000412_GR; LBUL_1983.
DR   KEGG; lbu:LBUL_1983; -.
DR   OMA; Q047K9; EWDTPNK.
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     80       D-alanine--poly(phosphoribitol) ligase
FT                                subunit 2.
FT                                /FTId=PRO_1000024916.
FT   MOD_RES      35     35       O-(pantetheine 4'-phosphoryl)serine
FT                                (Probable).
SQ   SEQUENCE   80 AA;  9259 MW;  7E04797CBF27A4FF CRC64;
     MDIQKQIVDI LAEATGEDFS DNMDQELYES GIMDSMTTVQ MLLTLQETFD ITVPVSEFNR
     DDWNTPNKLV EQVKKLQDEE
//