ID   LPTD_ECOL5              Reviewed;         784 AA.
AC   Q0TLT4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=ECP_0057;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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   -!- PTM: Contains two intramolecular disulfide bonds. {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; CP000247; ABG68097.1; -; Genomic_DNA.
DR   RefSeq; WP_000746171.1; NC_008253.1.
DR   AlphaFoldDB; Q0TLT4; -.
DR   SMR; Q0TLT4; -.
DR   STRING; 362663.ECP_0057; -.
DR   EnsemblBacteria; ABG68097; ABG68097; ECP_0057.
DR   KEGG; ecp:ECP_0057; -.
DR   HOGENOM; CLU_009039_2_0_6; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000009182; 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; Disulfide bond; Membrane; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           25..784
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281603"
FT   DISULFID        31..724
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   DISULFID        173..725
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
SQ   SEQUENCE   784 AA;  89653 MW;  6E9DBFD3C1F93C7E CRC64;
     MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL PVTINADHAK
     GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP VRTVDALGNV HYDDNQVILK
     GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILDNGSF TSCLPGSDTW
     SVVGSEIIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY
     FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYKD
     EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS TDGYATQKFS
     VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ NDVGPFDTRI YGQAVHFVNT
     RDDMPEATRV HLEPTINLPL SNNWGSINTE AKLLATHYQQ TNLDWYNSRN TTRLAESANR
     VMPQFKVDGR MVFERDMEML APGYTQTLEP RAQYLYVPYR DQSKIYNYDS SLLQSDYSGL
     FRDRTYGGLD RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND
     DKTGSLVWAG DTYWRISDRW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR LVQLNYRYAS
     PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV GAYYYDTNAN KQADSMLGVQ
     YSSCCYAIRV GYERKLNGWD NDKQHAVYDN AIGFNIELRG LSSNYGLGTQ EMLRSNILPY
     QNTL