LPTE_SALSV
ID LPTE_SALSV Reviewed; 196 AA.
AC B4TPX4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=SeSA_A0807;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(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}.
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; CP001127; ACF91886.1; -; Genomic_DNA.
DR RefSeq; WP_001269950.1; NC_011094.1.
DR AlphaFoldDB; B4TPX4; -.
DR SMR; B4TPX4; -.
DR EnsemblBacteria; ACF91886; ACF91886; SeSA_A0807.
DR KEGG; sew:SeSA_A0807; -.
DR HOGENOM; CLU_103309_1_1_6; -.
DR OMA; TTVNRNY; -.
DR Proteomes; UP000001865; 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_1000138281"
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