ID LPTE_ECOSM Reviewed; 193 AA.
AC B1LL90;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=EcSMS35_0661;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000970; ACB16201.1; -; Genomic_DNA.
DR RefSeq; WP_001269673.1; NC_010498.1.
DR AlphaFoldDB; B1LL90; -.
DR SMR; B1LL90; -.
DR GeneID; 75204998; -.
DR KEGG; ecm:EcSMS35_0661; -.
DR HOGENOM; CLU_103309_1_1_6; -.
DR Proteomes; UP000007011; 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_1000138272"
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
//
