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DLTC_STREM
ID   DLTC_STREM              Reviewed;          79 AA.
AC   B4U3P0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Sez_1269;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG62607.1; -; Genomic_DNA.
DR   RefSeq; WP_012515872.1; NC_011134.1.
DR   AlphaFoldDB; B4U3P0; -.
DR   SMR; B4U3P0; -.
DR   EnsemblBacteria; ACG62607; ACG62607; Sez_1269.
DR   GeneID; 64010842; -.
DR   KEGG; sez:Sez_1269; -.
DR   HOGENOM; CLU_108696_19_0_9; -.
DR   OMA; DEWNTPN; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000001873; 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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Phosphopantetheine;
KW   Phosphoprotein.
FT   CHAIN           1..79
FT                   /note="D-alanyl carrier protein"
FT                   /id="PRO_1000129401"
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"
SQ   SEQUENCE   79 AA;  9008 MW;  8A42B0BAA9E844E8 CRC64;
     MSTKETVIDL FDRLFMEDVS DMMDEDLFDA GVLDSLGTVE LIVEIESIFN IKVPISEFGR
     EDWNTANKII QGIEELQHA
 
 
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