LPTE_SHIFL
ID LPTE_SHIFL Reviewed; 193 AA.
AC Q83LX4; Q7C2L8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=SF0640, S0662;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- INTERACTION:
CC Q83LX4; Q83SQ0: lptD; NbExp=4; IntAct=EBI-16111649, EBI-16111665;
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; AE005674; AAN42276.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16147.1; -; Genomic_DNA.
DR RefSeq; NP_706569.1; NC_004337.2.
DR RefSeq; WP_001269672.1; NZ_UIQL01000006.1.
DR PDB; 4Q35; X-ray; 2.39 A; B=19-193.
DR PDBsum; 4Q35; -.
DR AlphaFoldDB; Q83LX4; -.
DR SMR; Q83LX4; -.
DR DIP; DIP-61035N; -.
DR IntAct; Q83LX4; 1.
DR STRING; 198214.SF0640; -.
DR DNASU; 1077092; -.
DR EnsemblBacteria; AAN42276; AAN42276; SF0640.
DR EnsemblBacteria; AAP16147; AAP16147; S0662.
DR GeneID; 1023631; -.
DR GeneID; 58390032; -.
DR KEGG; sfl:SF0640; -.
DR KEGG; sfx:S0662; -.
DR PATRIC; fig|198214.7.peg.747; -.
DR HOGENOM; CLU_103309_1_1_6; -.
DR OMA; TTVNRNY; -.
DR OrthoDB; 1685955at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; 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_0000281187"
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 HELIX 31..33
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4Q35"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 95..109
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4Q35"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:4Q35"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4Q35"
FT HELIX 133..157
FT /evidence="ECO:0007829|PDB:4Q35"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4Q35"
SQ SEQUENCE 193 AA; 21387 MW; C9387BD5308ADEDC CRC64;
MRYLATLLLS LAVLITAGCG WHLRDTTQVP STMKVMILDS GDPNGPLSRA VRNQLRLNGV
ELLDKETTRK DVPSLRLGKV SIAKDTASVF RNGQTAEYQM IMTVNATVLI PGRDIYPISA
KVFRSFFDNP QMALAKDNEQ DMIVKEMYDR AAEQLIRKLP SIRAADIRSD EEQTSTTTDT
PATPARVSTM LGN
