ID   LPTE_ECOL5              Reviewed;         193 AA.
AC   Q0TK32;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000255|HAMAP-Rule:MF_01186};
DE   Flags: Precursor;
GN   Name=lptE {ECO:0000255|HAMAP-Rule:MF_01186}; Synonyms=rlpB;
GN   OrderedLocusNames=ECP_0671;
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 LptD, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane. Required
CC       for the proper assembly of LptD. Binds LPS and may serve as the LPS
CC       recognition site at the outer membrane. {ECO:0000255|HAMAP-
CC       Rule:MF_01186}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptD. {ECO:0000255|HAMAP-Rule:MF_01186}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01186}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186}.
CC   -!- SIMILARITY: Belongs to the LptE lipoprotein family. {ECO:0000255|HAMAP-
CC       Rule:MF_01186}.
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DR   EMBL; CP000247; ABG68699.1; -; Genomic_DNA.
DR   RefSeq; WP_001269673.1; NC_008253.1.
DR   AlphaFoldDB; Q0TK32; -.
DR   SMR; Q0TK32; -.
DR   STRING; 362663.ECP_0671; -.
DR   EnsemblBacteria; ABG68699; ABG68699; ECP_0671.
DR   GeneID; 66671085; -.
DR   KEGG; ecp:ECP_0671; -.
DR   HOGENOM; CLU_103309_1_1_6; -.
DR   OMA; TTVNRNY; -.
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   HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR   InterPro; IPR007485; LPS_assembly_LptE.
DR   PANTHER; PTHR38098; PTHR38098; 1.
DR   Pfam; PF04390; LptE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01186"
FT   CHAIN           19..193
FT                   /note="LPS-assembly lipoprotein LptE"
FT                   /id="PRO_0000281179"
FT   REGION          166..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01186"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01186"
SQ   SEQUENCE   193 AA;  21357 MW;  C9387BC2008ADEDC CRC64;
     MRYLATLLLS LAVLITAGCG WHLRDTTQVP STMKVMILDS GDPNGPLSRA VRNQLRLNGV
     ELLDKETTRK DVPSLRLGKV SIAKDTASVF RNGQTAEYQM IMTVNATVLI PGRDIYPISA
     KVFRSFFDNP QMALAKDNEQ DMIVKEMYDR AAEQLIRKLP SIRAADIRSD EEQTSTTTDT
     PATPARVSTT LGN