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 27-MAR-2024, entry version 110.
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; Bacillota; 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 PaxDb; 321967-LSEI_0796; -.
DR GeneID; 57089408; -.
DR KEGG; lca:LSEI_0796; -.
DR PATRIC; fig|321967.11.peg.797; -.
DR HOGENOM; CLU_108696_19_0_9; -.
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; 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..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
//
