ID   DLTD_BACSU              Reviewed;         392 AA.
AC   P39578;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein DltD;
GN   Name=dltD; OrderedLocusNames=BSU38530; ORFNames=ipa-2r;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION.
RX   PubMed=7797557; DOI=10.1074/jbc.270.26.15598;
RA   Perego M., Glaser P., Minutello A., Strauch M.A., Leopold K., Fischer W.;
RT   "Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid
RT   in Bacillus subtilis. Identification of genes and regulation.";
RL   J. Biol. Chem. 270:15598-15606(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=27134729; DOI=10.12688/f1000research.8007.2;
RA   Luo Y.;
RT   "Alanylated lipoteichoic acid primer in Bacillus subtilis.";
RL   F1000Research 5:155-155(2016).
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:Q9RMN7, ECO:0000305|PubMed:27134729,
CC       ECO:0000305|PubMed:7797557}.
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC       {ECO:0000305|PubMed:7797557}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FZW3};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q2FZW3};
CC       Extracellular side {ECO:0000250|UniProtKB:Q2FZW3}.
CC   -!- SIMILARITY: Belongs to the DltD family. {ECO:0000305}.
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DR   EMBL; X73124; CAA51558.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15879.1; -; Genomic_DNA.
DR   PIR; S39657; S39657.
DR   RefSeq; NP_391732.1; NC_000964.3.
DR   RefSeq; WP_003227323.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39578; -.
DR   SMR; P39578; -.
DR   STRING; 224308.BSU38530; -.
DR   PaxDb; P39578; -.
DR   PRIDE; P39578; -.
DR   EnsemblBacteria; CAB15879; CAB15879; BSU_38530.
DR   GeneID; 937362; -.
DR   KEGG; bsu:BSU38530; -.
DR   PATRIC; fig|224308.179.peg.4172; -.
DR   eggNOG; COG3966; Bacteria.
DR   OMA; QMNWEEA; -.
DR   PhylomeDB; P39578; -.
DR   BioCyc; BSUB:BSU38530-MON; -.
DR   BioCyc; MetaCyc:BSU38530-MON; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000001570; Chromosome.
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; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..392
FT                   /note="Protein DltD"
FT                   /id="PRO_0000021107"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZW3"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..392
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZW3"
SQ   SEQUENCE   392 AA;  44809 MW;  0C0DA4673028B86E CRC64;
     MKKRFFGPII LAFILFAGAI AIPSSWLTGF ITDKRVKESA TALNPSMFQG LYLQDQMLKD
     PTYLPIYGSS ELSRLDEFHP SNYFQVNNEG FTPYLVGKGG SQSLIHSLNF AAHMDQLKGK
     KIVFIVSPQW FIKRGSDEQH FAPNYSALQG LDLAFNDQID PEIKKKMMKR MLRFKAVQND
     AILSELYKAM VNGQTWKVNA LKPAAKVYYS MLEKKDLYYS TTESSGPKRY ISQSVKDKSW
     SELNKLADQS GKRHSGSNDF HIDNPVYKKL KPKVPKLKGK NKGRSYAVSP EYGDFEMMLD
     ILKDAGAEPM FVTIPVNGKW YDYTGFPKKG RTDYYKKVNK QIRAKGFQVA DFSGHEYDPY
     FMKDTIHIGW KGWVYVDKAI DEFYKTGKVT SS