ID   LPTD_LEGPL              Reviewed;         839 AA.
AC   Q5WZN1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=lpl0350;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH14581.1; -; Genomic_DNA.
DR   RefSeq; WP_011214613.1; NC_006369.1.
DR   AlphaFoldDB; Q5WZN1; -.
DR   SMR; Q5WZN1; -.
DR   EnsemblBacteria; CAH14581; CAH14581; lpl0350.
DR   KEGG; lpf:lpl0350; -.
DR   LegioList; lpl0350; -.
DR   HOGENOM; CLU_009039_0_0_6; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000002517; Chromosome.
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   InterPro; IPR005653; OstA-like_N.
DR   Pfam; PF04453; LptD; 1.
DR   Pfam; PF03968; LptD_N; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           22..839
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281613"
SQ   SEQUENCE   839 AA;  95969 MW;  61F1258B2D5BF713 CRC64;
     MAIGITACVL SLINYQGLAY SAALINEPIQ ACVIAREVDL TDDIRTKFAQ CLGWQADQSS
     PVCLGFYKPI TVTPLASPDE VRILADTASF YRTQRSTLSG HVEMQQGQRV VNAQTAYVYR
     DPKTNEVTKI EFLNHVRYLE PDRMMIARKA VVYPQDKSGE VEDVLYRFNT NRSNALLPAW
     GRASLIKRFA NQDYFLKEAT YTTCAPQDKA WAIEAESISI NNEKGKGIAR NAKLRIHEWP
     VLYTPYLSFP TNRDRKSGFL MPIVGYSNVG GADLGIPYYW NMAPNYDMTL VPHIYTKRGL
     MLGGQFRYLT SKSTGTFNGN FLPKDKAFGR FLQDNEVEFP QIRGLSTNRW EVNFVDSTQF
     LSDLQLNVNF QQVSDDYYLQ DFSTNLASVT QRQLLRQADL TYTTENWTFR GMGQSYQTLH
     PINEIPVSPV YERLPQLMAR GYYDDLPFNA QLNILGQYDQ FHWPNDSWNI ALNNMPQGPR
     FHLNPILSVP MMKPWGYVTP SVQFVENYYD ISRNYTWGTS RANYNLTIPR YSLDGGLYFE
     RDLHLKGTYY IQTLEPRLFY LRVPYYNQTL IPVYDSGFMI FNVDQLFRTN RFSGFDRIGD
     ANQLSYALTT RWLEDESGAE KANFSIGQIK YFSERRVQLC QSPTGFCTDN PDTFGNLSST
     FGTSPVASRA VYKFNPAWGI TGDYIWDPAT RATNNADLNL HYQPARNAII NGGYSYLVNG
     DVTQVRNNDT ENNALHQAIL SAAWPLSEKW SGIGAYSYNI SKNYSMMSFL GVQYDSCCWA
     MRILGGRTFR SLNEEFEPRY NNNIYLQILL KGLGSVASSD PSGILNTYIP GYYDPFRRR