LPTD_ECOK1
ID LPTD_ECOK1 Reviewed; 784 AA.
AC A1A7A3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Ecok1_00490; ORFNames=APECO1_1928;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(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 -!- 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; CP000468; ABI99542.1; -; Genomic_DNA.
DR RefSeq; WP_000746170.1; NC_008563.1.
DR AlphaFoldDB; A1A7A3; -.
DR SMR; A1A7A3; -.
DR EnsemblBacteria; ABI99542; ABI99542; APECO1_1928.
DR KEGG; ecv:APECO1_1928; -.
DR HOGENOM; CLU_009039_2_0_6; -.
DR OMA; DYSHLDW; -.
DR Proteomes; UP000008216; 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_0000281602"
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; 89625 MW; B8A0B9E6C2C93244 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 TTKLAESANR
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