ID   LPTE_SALPA              Reviewed;         196 AA.
AC   Q5PM87;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=SPA2087;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
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DR   EMBL; CP000026; AAV77981.1; -; Genomic_DNA.
DR   RefSeq; WP_001269950.1; NC_006511.1.
DR   AlphaFoldDB; Q5PM87; -.
DR   SMR; Q5PM87; -.
DR   EnsemblBacteria; AAV77981; AAV77981; SPA2087.
DR   KEGG; spt:SPA2087; -.
DR   HOGENOM; CLU_103309_1_1_6; -.
DR   OMA; TTVNRNY; -.
DR   Proteomes; UP000008185; 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..196
FT                   /note="LPS-assembly lipoprotein LptE"
FT                   /id="PRO_0000281182"
FT   REGION          171..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..196
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   196 AA;  21431 MW;  427F294A2C464E29 CRC64;
     MRYLVTLLLS LAVLVTAGCG WHLRSTTQVP ASMKTMILDS GDPNGPLSRA VRNQLRLNNV
     NLLDKDTTRK DVPSLRLGTV TISQDTASVF QDGQTAEYQM VMTVNASVLI PGHDIYPIST
     KVYRSFFDNP QMALAKDNEQ AMIVQEMYDK AAEQLIRKLT SVRAADIQAT KEEATADNET
     AAPASTPARV STTLSN