ID   DLTC_STRT2              Reviewed;          79 AA.
AC   Q5M4V3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=stu0763;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH DLTB,
RP   PHOSPHOPANTETHEINYLATION AT SER-35, AND MUTAGENESIS OF SER-35 AND VAL-39.
RX   PubMed=30283133; DOI=10.1038/s41586-018-0568-2;
RA   Ma D., Wang Z., Merrikh C.N., Lang K.S., Lu P., Li X., Merrikh H., Rao Z.,
RA   Xu W.;
RT   "Crystal structure of a membrane-bound O-acyltransferase.";
RL   Nature 562:286-290(2018).
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       ECO:0000305|PubMed:30283133}.
CC   -!- SIMILARITY: Belongs to the DltC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00565}.
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DR   EMBL; CP000023; AAV60454.1; -; Genomic_DNA.
DR   RefSeq; WP_002950439.1; NC_006448.1.
DR   PDB; 6BUG; X-ray; 3.27 A; A/B/E=1-79.
DR   PDB; 6BUH; X-ray; 3.15 A; A/B/E/G=1-79.
DR   PDBsum; 6BUG; -.
DR   PDBsum; 6BUH; -.
DR   AlphaFoldDB; Q5M4V3; -.
DR   SMR; Q5M4V3; -.
DR   STRING; 264199.stu0763; -.
DR   EnsemblBacteria; AAV60454; AAV60454; stu0763.
DR   GeneID; 66898661; -.
DR   KEGG; stl:stu0763; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_19_0_9; -.
DR   OMA; DEWNTPN; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000001170; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Cytoplasm;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..79
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_1000024938"
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,
FT                   ECO:0000305|PubMed:30283133"
FT   MUTAGEN         35
FT                   /note="S->A: Does not affect binding to DltC."
FT                   /evidence="ECO:0000269|PubMed:30283133"
FT   MUTAGEN         39
FT                   /note="V->D,R: Reduced binding to DltB."
FT                   /evidence="ECO:0000269|PubMed:30283133"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   TURN            27..31
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   HELIX           37..49
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:6BUH"
FT   HELIX           66..78
FT                   /evidence="ECO:0007829|PDB:6BUH"
SQ   SEQUENCE   79 AA;  8969 MW;  82F000B1735AAD8D CRC64;
     MDVKAEVIEI IDELFMEDVS DMMDEDLFDA GVLDSMGTVE LIVELESRFD IRVPVSEFGR
     DDWNTANKIV EGVTELRNA