ID   DLTC_STAXY              Reviewed;          78 AA.
AC   Q9X2N6;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=D-alanyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00565};
DE            Short=DCP {ECO:0000255|HAMAP-Rule:MF_00565};
DE   AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00565};
GN   Name=dltC {ECO:0000255|HAMAP-Rule:MF_00565};
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   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 peptides.";
RL   J. Biol. Chem. 274:8405-8410(1999).
CC   -!- FUNCTION: Carrier protein involved in the D-alanylation of lipoteichoic
CC       acid (LTA). The loading of thioester-linked D-alanine onto DltC is
CC       catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-
CC       carried D-alanyl group is further transferred to cell membrane
CC       phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed
CC       by DltD. D-alanylation of LTA plays an important role in modulating the
CC       properties of the cell wall in Gram-positive bacteria, influencing the
CC       net charge of the cell wall. {ECO:0000255|HAMAP-Rule:MF_00565}.
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00565}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00565}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-DCP. {ECO:0000255|HAMAP-Rule:MF_00565}.
CC   -!- SIMILARITY: Belongs to the DltC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00565}.
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DR   EMBL; AF032440; AAD01944.1; -; Genomic_DNA.
DR   RefSeq; WP_047172668.1; NZ_QXUB01000010.1.
DR   AlphaFoldDB; Q9X2N6; -.
DR   SMR; Q9X2N6; -.
DR   STRING; 1288.SXYLSMQ121_1841; -.
DR   KEGG; sxo:SXYL_01988; -.
DR   eggNOG; COG0236; Bacteria.
DR   UniPathway; UPA00556; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036370; F:D-alanyl carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   HAMAP; MF_00565; DltC; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003230; DltC.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR01688; dltC; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Phosphopantetheine;
KW   Phosphoprotein.
FT   CHAIN           1..78
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_0000213108"
FT   DOMAIN          1..78
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT   MOD_RES         36
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
SQ   SEQUENCE   78 AA;  9155 MW;  C64B76620E7074C2 CRC64;
     MEFREQVLDL LTEVAENNVI KENPDVELFE EGIFDSFQTV GLLLEIQNKL DIEVSIMDFD
     RDEWATPNKI VEVLEELR