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Database: UniProt
Entry: B6I152
LinkDB: B6I152
Original site: B6I152 
ID   LPTE_ECOSE              Reviewed;         193 AA.
AC   B6I152;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=ECSE_0710;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG76234.1; -; Genomic_DNA.
DR   RefSeq; WP_001269673.1; NC_011415.1.
DR   AlphaFoldDB; B6I152; -.
DR   SMR; B6I152; -.
DR   GeneID; 75204998; -.
DR   KEGG; ecy:ECSE_0710; -.
DR   HOGENOM; CLU_103309_1_1_6; -.
DR   Proteomes; UP000008199; 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   Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR   HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR   InterPro; IPR007485; LPS_assembly_LptE.
DR   PANTHER; PTHR38098; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR   PANTHER; PTHR38098:SF1; LPS-ASSEMBLY LIPOPROTEIN LPTE; 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_1000138271"
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
//
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