ID DLTC_STAA3 Reviewed; 78 AA. AC Q2FIE1; 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 2; DE EC=6.1.1.13; DE AltName: Full=D-alanyl carrier protein; DE Short=DCP; GN Name=dltC; OrderedLocusNames=SAUSA300_0837; 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). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000255; ABD20609.1; -; Genomic_DNA. DR RefSeq; YP_493537.1; -. DR GeneID; 3912974; -. DR GenomeReviews; CP000255_GR; SAUSA300_0837. DR KEGG; saa:SAUSA300_0837; -. DR HOGENOM; Q2FIE1; -. DR OMA; Q2FIE1; 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 78 D-alanine--poly(phosphoribitol) ligase FT subunit 2. FT /FTId=PRO_1000024924. 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 //