ID   DLTC_STRS2              Reviewed;          79 AA.
AC   A4W0A9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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}; OrderedLocusNames=SSU98_0640;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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; CP000408; ABP91798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4W0A9; -.
DR   SMR; A4W0A9; -.
DR   KEGG; ssv:SSU98_0640; -.
DR   HOGENOM; CLU_108696_19_0_9; -.
DR   OMA; DEWNTPN; -.
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..79
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_1000024934"
FT   DOMAIN          1..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT   MOD_RES         35
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
SQ   SEQUENCE   79 AA;  8939 MW;  FAD5546FE95D8067 CRC64;
     MDVKETILNI IQELFMEDVS EMMDEDLLHA GVLDSMGTVE LIVELESRFN ITVPVSEFGR
     EDWNTANKII SGVVELMHA