ID   DLTC_LACRH              Reviewed;          81 AA.
AC   P55153;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 120.
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   Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC   / NCIMB 6375 / NCTC 12953;
RX   PubMed=8682792; DOI=10.1128/jb.178.13.3869-3876.1996;
RA   Debabov D.V., Heaton M.P., Zhang Q., Stewart K., Lambalot R.H.,
RA   Neuhaus F.C.;
RT   "The D-alanyl carrier protein in Lactobacillus casei: cloning, sequencing,
RT   and expression of dltC.";
RL   J. Bacteriol. 178:3869-3876(1996).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=11222605; DOI=10.1128/jb.183.6.2051-2058.2001;
RA   Kiriukhin M.Y., Neuhaus F.C.;
RT   "D-alanylation of lipoteichoic acid: role of the D-alanyl carrier protein
RT   in acylation.";
RL   J. Bacteriol. 183:2051-2058(2001).
RN   [3]
RP   STRUCTURE BY NMR OF 2-81.
RX   PubMed=11434765; DOI=10.1021/bi010355a;
RA   Volkman B.F., Zhang Q., Debabov D.V., Rivera E., Kresheck G.C.,
RA   Neuhaus F.C.;
RT   "Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-
RT   D-alanyl carrier protein.";
RL   Biochemistry 40:7964-7972(2001).
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; U43894; AAB17659.1; -; Genomic_DNA.
DR   RefSeq; WP_005685531.1; NZ_WPCQ01000011.1.
DR   PDB; 1DV5; NMR; -; A=2-81.
DR   PDBsum; 1DV5; -.
DR   AlphaFoldDB; P55153; -.
DR   BMRB; P55153; -.
DR   SMR; P55153; -.
DR   STRING; 568703.LGG_00779; -.
DR   eggNOG; COG0236; Bacteria.
DR   OMA; DEWNTPN; -.
DR   UniPathway; UPA00556; -.
DR   EvolutionaryTrace; P55153; -.
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.
FT   CHAIN           1..81
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_0000213093"
FT   DOMAIN          1..81
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT   MOD_RES         39
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:1DV5"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1DV5"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:1DV5"
FT   HELIX           40..49
FT                   /evidence="ECO:0007829|PDB:1DV5"
FT   TURN            64..68
FT                   /evidence="ECO:0007829|PDB:1DV5"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:1DV5"
SQ   SEQUENCE   81 AA;  8920 MW;  42696C57B286D46D CRC64;
     MADEAIKNGV LDILADLTGS DDVKKNLDLN LFETGLLDSM GTVQLLLELQ SQFGVDAPVS
     EFDRKEWDTP NKIIAKVEQA Q