ID DLTC1_LACPL Reviewed; 80 AA.
AC Q88VM8; F9UPX6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-NOV-2024, entry version 116.
DE RecName: Full=D-alanyl carrier protein 1 {ECO:0000255|HAMAP-Rule:MF_00565};
DE Short=DCP 1 {ECO:0000255|HAMAP-Rule:MF_00565};
DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 2-1 {ECO:0000255|HAMAP-Rule:MF_00565};
GN Name=dltC1 {ECO:0000255|HAMAP-Rule:MF_00565}; OrderedLocusNames=lp_2017;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79265.1; -; Genomic_DNA.
DR RefSeq; WP_003640705.1; NC_004567.2.
DR RefSeq; YP_004889779.1; NC_004567.2.
DR PDB; 7R49; X-ray; 1.88 A; E/F/H=1-80.
DR PDBsum; 7R49; -.
DR AlphaFoldDB; Q88VM8; -.
DR SMR; Q88VM8; -.
DR STRING; 220668.lp_2017; -.
DR EnsemblBacteria; CCC79265; CCC79265; lp_2017.
DR GeneID; 89669304; -.
DR KEGG; lpl:lp_2017; -.
DR PATRIC; fig|220668.9.peg.1704; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_19_0_9; -.
DR OrthoDB; 6462171at2; -.
DR PhylomeDB; Q88VM8; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000432; 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; ACP-like; 1.
DR HAMAP; MF_00565; DltC; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003230; DltC.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01688; dltC; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 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..80
FT /note="D-alanyl carrier protein 1"
FT /id="PRO_0000213091"
FT DOMAIN 1..80
FT /note="Carrier"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT MOD_RES 38
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:7R49"
FT TURN 30..34
FT /evidence="ECO:0007829|PDB:7R49"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:7R49"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7R49"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:7R49"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7R49"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:7R49"
SQ SEQUENCE 80 AA; 8798 MW; B32C0E48E1B8ED08 CRC64;
MTMDDTKATV LSILADLTGE DVSSNMDVNL FDEGILDSMG SVQLLLELQN QLGIEVPVSE
FQRSEWDTPA KIVAKVENLQ
//
