ID   LPTD_FRAT1              Reviewed;         868 AA.
AC   Q14IY9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=FTF0467;
OS   Francisella tularensis subsp. tularensis (strain FSC 198).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC 198;
RX   PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA   Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA   Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA   Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT   "Genome sequencing shows that European isolates of Francisella tularensis
RT   subspecies tularensis are almost identical to US laboratory strain Schu
RT   S4.";
RL   PLoS ONE 2:E352-E352(2007).
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; AM286280; CAL08483.1; -; Genomic_DNA.
DR   RefSeq; WP_003023202.1; NC_008245.1.
DR   AlphaFoldDB; Q14IY9; -.
DR   SMR; Q14IY9; -.
DR   KEGG; ftf:FTF0467; -.
DR   HOGENOM; CLU_009039_1_0_6; -.
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   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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           25..868
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281608"
SQ   SEQUENCE   868 AA;  98401 MW;  D1D062F1237D2B36 CRC64;
     MLKGIHKYLL MCFGTVLFTV QANAARIMSN NPIKEDWQCK VVDGEWSCKR AKKPKSVFDK
     KLTKTEKEKA LADDLAWVKK PSYFVGGYYS NDNQFTKALC ESKKTDLSYE KSEFDNYGTL
     IASGNVQVLQ CDQELYGNNA IINLNSNNSA IRSLVMAGDV IVKQPSTGIV IRTTELDADM
     NNGTYSTGEA YFRLAREMPK TRIYDKEHFS GYLRGYAKTF KKESSGDIVL SDGYITSGDP
     YDNAWKITGN NIDIDTNTHM AYVKNGYFEI QDIPVMYIPY FSHPIDDRRR SGFLYPGFVQ
     NANSGIGISV PYYFNLAPNY DLMLQSVIWS QRGIIENGTF RYMTKYFQGQ FEGSLVPYDF
     KEGKMRGSFT LSTTGQYENI NTNFKYEYVS DQNYYNDFSA GNVNLVTKTL LDREFDLTYT
     NDYVDSGLTV LDYGVVNPLL TVDNTPYAKL PEVKLNLTSD GYTPDYLTLS AQTLNTFFYK
     TAGPANTNPG APQGTNVNAF RAYESPKIAF NFNKTWGYLN PSLEVPIRYY QLKNSPTDTI
     QFANSSVTSV LPIFNIDAGA YFDKDYTNEN GTYTSTLHPR LFYTYIPYQD QTNIPLFDTS
     LQNEQYMQMF QVNRFTGYDR INNANQLTYA IEASTTNQDN GTTLASAKIG QMAYFADRKV
     NLCQGNSACP NPGLMDPFST DTFSPIMSSF EFQVMKNIYL SAQVNYRVNQ QNVDYQVYQL
     SYKDENENIF NVSYNNIANN WNSLTQQQIA EGAKPQPQET ITLSTVLNIT DHWGIAALWN
     YNFQQKQIAN IFAGLQYNAK SWAVRALWQK TAYTNQDPNN PTLLGPLVNT YMFEFELKGL
     GGIGNTSDIS SRLQQINGYQ VGEWGNGI