LPTE_ECOK1
ID LPTE_ECOK1 Reviewed; 193 AA.
AC A1A8R6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Ecok1_05620; ORFNames=APECO1_1414;
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 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; CP000468; ABJ00056.1; -; Genomic_DNA.
DR RefSeq; WP_001269673.1; NC_008563.1.
DR AlphaFoldDB; A1A8R6; -.
DR SMR; A1A8R6; -.
DR EnsemblBacteria; ABJ00056; ABJ00056; APECO1_1414.
DR GeneID; 66671085; -.
DR KEGG; ecv:APECO1_1414; -.
DR HOGENOM; CLU_103309_1_1_6; -.
DR OMA; TTVNRNY; -.
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 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_0000281178"
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