DLTC_LEUMM
ID DLTC_LEUMM Reviewed; 78 AA.
AC Q03V70;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=LEUM_1815;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
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; CP000414; ABJ62902.1; -; Genomic_DNA.
DR RefSeq; WP_010292689.1; NC_008531.1.
DR AlphaFoldDB; Q03V70; -.
DR SMR; Q03V70; -.
DR STRING; 203120.LEUM_1815; -.
DR EnsemblBacteria; ABJ62902; ABJ62902; LEUM_1815.
DR GeneID; 61177770; -.
DR KEGG; lme:LEUM_1815; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_19_0_9; -.
DR OMA; DEWNTPN; -.
DR OrthoDB; 1943389at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000362; 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..78
FT /note="D-alanyl carrier protein"
FT /id="PRO_1000024921"
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 78 AA; 8845 MW; 9CB81E8163BB9272 CRC64;
MDLKEQIVEI LNTIIGEDIS DQMDDDFFEN GLLDSMATVE LLLDLESKFN IQAPVSEFNR
DEWNTPNKVV AKVESLIG