ID   DLTC_LACP3              Reviewed;          81 AA.
AC   Q03AZ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=LSEI_0796;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000423; ABJ69632.1; -; Genomic_DNA.
DR   RefSeq; WP_003564027.1; NC_008526.1.
DR   RefSeq; YP_806074.1; NC_008526.1.
DR   PDB; 1HQB; NMR; -; A=2-81.
DR   PDBsum; 1HQB; -.
DR   AlphaFoldDB; Q03AZ0; -.
DR   SMR; Q03AZ0; -.
DR   STRING; 321967.LSEI_0796; -.
DR   EnsemblBacteria; ABJ69632; ABJ69632; LSEI_0796.
DR   GeneID; 61269018; -.
DR   KEGG; lca:LSEI_0796; -.
DR   PATRIC; fig|321967.11.peg.797; -.
DR   HOGENOM; CLU_108696_19_0_9; -.
DR   OMA; DEWNTPN; -.
DR   UniPathway; UPA00556; -.
DR   EvolutionaryTrace; Q03AZ0; -.
DR   Proteomes; UP000001651; 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.
FT   CHAIN           1..81
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_1000024914"
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:1HQB"
FT   TURN            21..25
FT                   /evidence="ECO:0007829|PDB:1HQB"
FT   TURN            31..34
FT                   /evidence="ECO:0007829|PDB:1HQB"
FT   HELIX           40..49
FT                   /evidence="ECO:0007829|PDB:1HQB"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:1HQB"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1HQB"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:1HQB"
SQ   SEQUENCE   81 AA;  8865 MW;  24DBFC59AD86D47C CRC64;
     MADEAIKNGV LDILADLTGS DDVKTNLDLN LFETGLLDSM GTVQLLLELQ SQFGVEAPVS
     EFDRSQWDTP NKIIAKVEQA Q