ID   LPTD_BURCA              Reviewed;         786 AA.
AC   Q1BTQ5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE   Flags: Precursor;
GN   Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA;
GN   OrderedLocusNames=Bcen_2099;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with LptE, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01411}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptE and LptA. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
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DR   EMBL; CP000378; ABF77000.1; -; Genomic_DNA.
DR   RefSeq; WP_011546173.1; NC_008060.1.
DR   AlphaFoldDB; Q1BTQ5; -.
DR   SMR; Q1BTQ5; -.
DR   EnsemblBacteria; ABF77000; ABF77000; Bcen_2099.
DR   KEGG; bcn:Bcen_2099; -.
DR   HOGENOM; CLU_009039_0_0_4; -.
DR   OMA; DYSHLDW; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro.
DR   GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR   HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR   InterPro; IPR020889; LipoPS_assembly_LptD.
DR   InterPro; IPR007543; LptD_C.
DR   Pfam; PF04453; LptD; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           40..786
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_5000123058"
FT   REGION          767..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  86936 MW;  E9CE6230DD1A12B2 CRC64;
     MPPKPLFPNV FPGDGAPRKR RLALALLAVP GLVPAVSYAQ LSGAAAQPQP LDSPWDLRLA
     PQLEDHPLKD GAKPAAFVIA DHTSGTAEQD LAAKGSAELR RGDAVVKADA IHYDQDTDMA
     DAYGQVKVIN GGTSFAGPEA HLKIEANQGF MTAPKYHFNV TGGSGSAERV DMVDNERSVF
     VNGTYTACQC STNPAWYIKG SRFDFDTGAD EGTARNGVLF FQGVPIFASP WMTFPLSGER
     RSGLLPPTFS MNSSNGFELS LPYYFNIAPN RDLTLTPRII SRRGVMTEAT FRYLSPSYSG
     TFTANYLPDD RLAHRNRYAI YWQHQQNFGG GFGGYVYYNK VSDNTYPEDL GSANQFINGT
     QTLYQQEAGL TYNNGPWSVL ARYQHWQTLP PSIAPYSREP QLNVKYTKYN VGGFDFGAEA
     DYSRFRITTA DATEGDRIVF NPYISYGVYG PGYFVVPKVQ YHFASYDLNY LSSTTPNSPK
     RFTESIPTVT FDTGLIFDRS VRLFGQDFIQ TLEPRLYYVY TPYRDQSNAP LFDTAESDFG
     LAEIYQPNTF VGNDRIADAN RITAGLTSRF IDPRTGDERA RFVIAQQYYF ADQRVTLNPG
     QAAVLARHSD LIVGAALKLG SGFMSETAFQ YNQNNNQLVK SSVGFGYSPG ERRVINVGYR
     YTRANTTLDN QPINQFLVSA QWPLTRRLYA IGRFNYDLAG DRVVDGLVGL QYDADCWALG
     VGVQRAANGI NSSGQQNSST RFMMQLTLKG LSTVDNGLVS AFRAGVPGYT PLPPPPPPMS
     RFSNYE