LPTE_ECOUT
ID LPTE_ECOUT Reviewed; 193 AA.
AC Q1RES0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=UTI89_C0644;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE06144.1; -; Genomic_DNA.
DR RefSeq; WP_001269673.1; NC_007946.1.
DR AlphaFoldDB; Q1RES0; -.
DR SMR; Q1RES0; -.
DR EnsemblBacteria; ABE06144; ABE06144; UTI89_C0644.
DR GeneID; 66671085; -.
DR KEGG; eci:UTI89_C0644; -.
DR HOGENOM; CLU_103309_1_1_6; -.
DR OMA; TTVNRNY; -.
DR Proteomes; UP000001952; 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_0000281176"
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