ID   DLTD_LACRH              Reviewed;         423 AA.
AC   P55154; Q9RMN7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Protein DltD;
GN   Name=dltD;
OS   Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   PATHWAY.
RC   STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC   / NCIMB 6375 / NCTC 12953;
RX   PubMed=10781555; DOI=10.1128/jb.182.10.2855-2864.2000;
RA   Debabov D.V., Kiriukhin M.Y., Neuhaus F.C.;
RT   "Biosynthesis of lipoteichoic acid in Lactobacillus rhamnosus: role of DltD
RT   in D-alanylation.";
RL   J. Bacteriol. 182:2855-2864(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
RC   STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC   / NCIMB 6375 / NCTC 12953;
RX   PubMed=8682792; DOI=10.1128/jb.178.13.3869-3876.1996;
RA   Debabov D.V., Heaton M.P., Zhang Q., Stewart K., Lambalot R.H.,
RA   Neuhaus F.C.;
RT   "The D-alanyl carrier protein in Lactobacillus casei: cloning, sequencing,
RT   and expression of dltC.";
RL   J. Bacteriol. 178:3869-3876(1996).
CC   -!- FUNCTION: Involved in the D-alanylation of lipoteichoic acid (LTA).
CC       Could be responsible for the transfer of DltC-carried D-alanyl groups
CC       to cell membrane phosphatidylglycerol (PG), or alternatively of D-
CC       alanine residues from D-Ala-undecaprenol phosphate to the
CC       poly(glycerophosphate) chains of LTA. D-alanylation of LTA plays an
CC       important role in modulating the properties of the cell wall in Gram-
CC       positive bacteria, influencing the net charge of the cell wall.
CC       {ECO:0000250|UniProtKB:P39578, ECO:0000305|PubMed:10781555}.
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC       {ECO:0000305|PubMed:10781555}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10781555};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:10781555};
CC       Extracellular side {ECO:0000250|UniProtKB:Q2FZW3}.
CC   -!- SIMILARITY: Belongs to the DltD family. {ECO:0000305}.
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DR   EMBL; AF192553; AAF09204.1; -; Genomic_DNA.
DR   EMBL; U43894; AAB17660.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55154; -.
DR   SMR; P55154; -.
DR   STRING; 568703.LGG_00780; -.
DR   PRIDE; P55154; -.
DR   eggNOG; COG3966; Bacteria.
DR   UniPathway; UPA00556; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006998; DltD.
DR   InterPro; IPR023896; LTA_DltD.
DR   PANTHER; PTHR40039; PTHR40039; 1.
DR   Pfam; PF04914; DltD; 1.
DR   PIRSF; PIRSF021438; DltD; 1.
DR   TIGRFAMs; TIGR04092; LTA_DltD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..423
FT                   /note="Protein DltD"
FT                   /id="PRO_0000021108"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZW3"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..423
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZW3"
FT   CONFLICT        65
FT                   /note="E -> D (in Ref. 2; AAB17660)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="V -> L (in Ref. 2; AAB17660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   423 AA;  47990 MW;  18B11CEAA3D1FAF7 CRC64;
     MKKPIGKILW RGLGPLLIAI ILVAALMLVP FKFGRSSQAT IRQAASSMSA NVLKGETIKN
     EAMAENYVPF IGSSELSRMD AFHPSVLAQK YHRDYRPFLM GMAGSQSLTH FLSINALTHV
     EGKKAVMVLS PQWFVPGGVR KAQFDYFYSP AQMTTFLLHA NPNSEADRFA ARRLLQFPST
     DSDRTVNEAL KNIAAGQKLS DGQYWYLKQV KDPMADHQDA LFSRLFLNNN QPQLDKAAKT
     LPSTYDVDDL DGLATRMGMQ ETTNNPFELK NDFYTKRVKR NMPKLKGSQA TWSYVKSPEY
     SDLQLVLNTF AKKHMEVLFV IPPINAKWAA FTGLDLGMIQ NTVTKMKYQL KTQGFNHVLD
     LSQDGAQPYF MEDTIHIGWR GWLKMDQTVR PFLKTTKAAP VHYKLNDQFY TKHWQQQSAN
     GLD