LPTE_ECOLI
ID LPTE_ECOLI Reviewed; 193 AA.
AC P0ADC1; P10101; P77576;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000255|HAMAP-Rule:MF_01186};
DE AltName: Full=Rare lipoprotein B;
DE Flags: Precursor;
GN Name=lptE {ECO:0000255|HAMAP-Rule:MF_01186}; Synonyms=rlpB;
GN OrderedLocusNames=b0641, JW0636;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], LIPOPROTEIN, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=3316191; DOI=10.1128/jb.169.12.5692-5699.1987;
RA Takase I., Ishino F., Wachi M., Kamata H., Doi M., Asoh S., Matsuzawa H.,
RA Ohta T., Matsuhashi M.;
RT "Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia
RT coli chromosome.";
RL J. Bacteriol. 169:5692-5699(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH LPTD.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16861298; DOI=10.1073/pnas.0604744103;
RA Wu T., McCandlish A.C., Gronenberg L.S., Chng S.-S., Silhavy T.J.,
RA Kahne D.;
RT "Identification of a protein complex that assembles lipopolysaccharide in
RT the outer membrane of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11754-11759(2006).
RN [7]
RP FUNCTION, AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=18424520; DOI=10.1128/jb.00270-08;
RA Sperandeo P., Lau F.K., Carpentieri A., De Castro C., Molinaro A., Deho G.,
RA Silhavy T.J., Polissi A.;
RT "Functional analysis of the protein machinery required for transport of
RT lipopolysaccharide to the outer membrane of Escherichia coli.";
RL J. Bacteriol. 190:4460-4469(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20446753; DOI=10.1021/bi100493e;
RA Chng S.S., Gronenberg L.S., Kahne D.;
RT "Proteins required for lipopolysaccharide assembly in Escherichia coli form
RT a transenvelope complex.";
RL Biochemistry 49:4565-4567(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH LPTD.
RX PubMed=20203010; DOI=10.1073/pnas.0912872107;
RA Chng S.S., Ruiz N., Chimalakonda G., Silhavy T.J., Kahne D.;
RT "Characterization of the two-protein complex in Escherichia coli
RT responsible for lipopolysaccharide assembly at the outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5363-5368(2010).
RN [10]
RP INTERACTION WITH LPTD, AND SUBCELLULAR LOCATION.
RX PubMed=21257904; DOI=10.1073/pnas.1015617108;
RA Freinkman E., Chng S.S., Kahne D.;
RT "The complex that inserts lipopolysaccharide into the bacterial outer
RT membrane forms a two-protein plug-and-barrel.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2486-2491(2011).
RN [11]
RP INTERACTION WITH LPTD, AND MUTAGENESIS OF 117-PRO--SER-119.
RX PubMed=21257909; DOI=10.1073/pnas.1019089108;
RA Chimalakonda G., Ruiz N., Chng S.S., Garner R.A., Kahne D., Silhavy T.J.;
RT "Lipoprotein LptE is required for the assembly of LptD by the beta-barrel
RT assembly machine in the outer membrane of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2492-2497(2011).
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, ECO:0000269|PubMed:16861298,
CC ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20203010}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptD. May interact with LptD during its
CC assembly by the beta-barrel assembly machine. Directly contacts LptD at
CC a wide range of positions, encompassing multiple surfaces of LptE. In
CC one specific interaction, LptE contacts a predicted extracellular loop
CC of LptD through the lumen of the beta-barrel. This specific interaction
CC is required for proper folding of LptD and assembly of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:16861298,
CC ECO:0000269|PubMed:20203010, ECO:0000269|PubMed:21257904,
CC ECO:0000269|PubMed:21257909}.
CC -!- INTERACTION:
CC P0ADC1; P31554: lptD; NbExp=19; IntAct=EBI-1119442, EBI-549369;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01186, ECO:0000269|PubMed:20446753,
CC ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:20446753,
CC ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}. Note=A
CC substantial portion is found inside the LptD beta-barrel.
CC -!- SIMILARITY: Belongs to the LptE lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_01186}.
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DR EMBL; M18277; AAA24554.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40842.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73742.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35288.1; -; Genomic_DNA.
DR PIR; G64798; LPECRB.
DR RefSeq; NP_415174.1; NC_000913.3.
DR RefSeq; WP_001269673.1; NZ_STEB01000031.1.
DR PDB; 4NHR; X-ray; 2.34 A; A=20-182.
DR PDB; 4RH8; X-ray; 2.20 A; A/B/C/D=20-186.
DR PDB; 4RHB; X-ray; 3.35 A; B/D=19-193.
DR PDBsum; 4NHR; -.
DR PDBsum; 4RH8; -.
DR PDBsum; 4RHB; -.
DR AlphaFoldDB; P0ADC1; -.
DR SMR; P0ADC1; -.
DR BioGRID; 4260757; 230.
DR ComplexPortal; CPX-1093; LptDE outer membrane translocon complex.
DR DIP; DIP-35987N; -.
DR IntAct; P0ADC1; 6.
DR STRING; 511145.b0641; -.
DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family.
DR jPOST; P0ADC1; -.
DR PaxDb; P0ADC1; -.
DR PRIDE; P0ADC1; -.
DR EnsemblBacteria; AAC73742; AAC73742; b0641.
DR EnsemblBacteria; BAA35288; BAA35288; BAA35288.
DR GeneID; 66671085; -.
DR GeneID; 946257; -.
DR KEGG; ecj:JW0636; -.
DR KEGG; eco:b0641; -.
DR PATRIC; fig|1411691.4.peg.1627; -.
DR EchoBASE; EB0848; -.
DR eggNOG; COG2980; Bacteria.
DR HOGENOM; CLU_103309_1_1_6; -.
DR OMA; TTVNRNY; -.
DR PhylomeDB; P0ADC1; -.
DR BioCyc; EcoCyc:EG10855-MON; -.
DR BioCyc; MetaCyc:EG10855-MON; -.
DR PRO; PR:P0ADC1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:1990351; C:transporter complex; IDA:EcoCyc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IMP:EcoCyc.
DR GO; GO:0015920; P:lipopolysaccharide transport; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT CHAIN 19..193
FT /note="LPS-assembly lipoprotein LptE"
FT /id="PRO_0000018185"
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"
FT MUTAGEN 117..119
FT /note="PIS->R: Affects interaction with LptD and LptD
FT biogenesis. Increases outer membrane permeability."
FT /evidence="ECO:0000269|PubMed:21257909"
FT CONFLICT 117
FT /note="P -> S (in Ref. 1; AAA24554)"
FT /evidence="ECO:0000305"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4RH8"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4RH8"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:4RH8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4RH8"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4NHR"
FT STRAND 74..110
FT /evidence="ECO:0007829|PDB:4RH8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4RH8"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:4RH8"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4NHR"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:4RH8"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4RH8"
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
