(data stored in ACNUC7421 zone)

SWISSPROT: LPTE_ECO27

ID   LPTE_ECO27              Reviewed;         193 AA.
AC   B7UKT1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
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=E2348C_0541;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Together with LptD, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane.
CC       Required for the proper assembly of LptD. Binds LPS and may serve
CC       as the LPS recognition site at the outer membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01186}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and
CC       assembly complex. Interacts with LptD. {ECO:0000255|HAMAP-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_01186}.
DR   EMBL; FM180568; CAS08089.1; -; Genomic_DNA.
DR   RefSeq; WP_001269673.1; NC_011601.1.
DR   SMR; B7UKT1; -.
DR   EnsemblBacteria; CAS08089; CAS08089; E2348C_0541.
DR   KEGG; ecg:E2348C_0541; -.
DR   KO; K03643; -.
DR   OMA; GDPYGPL; -.
DR   BioCyc; ECOL574521:E2348C_RS02845-MONOMER; -.
DR   Proteomes; UP000008205; 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;
DR   PRODOM; B7UKT1.
DR   SWISS-2DPAGE; B7UKT1.
KW   Cell outer membrane; Complete proteome; Lipoprotein; Membrane;
KW   Palmitate; Signal.
FT   SIGNAL        1     18       {ECO:0000255|HAMAP-Rule:MF_01186}.
FT   CHAIN        19    193       LPS-assembly lipoprotein LptE.
FT                                /FTId=PRO_1000164473.
FT   LIPID        19     19       N-palmitoyl cysteine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01186}.
FT   LIPID        19     19       S-diacylglycerol cysteine.
FT                                {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
//

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