DLTC_LACLS
ID DLTC_LACLS Reviewed; 79 AA.
AC Q02YS9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=LACR_1372;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11;
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; CP000425; ABJ72893.1; -; Genomic_DNA.
DR RefSeq; WP_011676184.1; NC_008527.1.
DR AlphaFoldDB; Q02YS9; -.
DR SMR; Q02YS9; -.
DR EnsemblBacteria; ABJ72893; ABJ72893; LACR_1372.
DR GeneID; 61109507; -.
DR KEGG; llc:LACR_1372; -.
DR HOGENOM; CLU_108696_19_0_9; -.
DR OMA; DEWNTPN; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000240; 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_1000024919"
FT DOMAIN 1..76
FT /note="Carrier"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT MOD_RES 34
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
SQ SEQUENCE 79 AA; 9126 MW; 118E93C94AE9026B CRC64;
MKEQIFDIIE TISGTDEFRE DLDMDLFEEG ILDSMRAIML IVELEGAFDI SLPPSEMDRE
DWNTANKIAA RVQEKTDEN