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Database: UniProt
Entry: B1KDW1_SHEWM
LinkDB: B1KDW1_SHEWM
Original site: B1KDW1_SHEWM 
ID   B1KDW1_SHEWM            Unreviewed;       164 AA.
AC   B1KDW1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
DE   Flags: Precursor;
GN   Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN   OrderedLocusNames=Swoo_3703 {ECO:0000313|EMBL:ACA87963.1};
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87963.1, ECO:0000313|Proteomes:UP000002168};
RN   [1] {ECO:0000313|EMBL:ACA87963.1, ECO:0000313|Proteomes:UP000002168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_01186}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptD. {ECO:0000256|HAMAP-Rule:MF_01186}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01186}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_01186}.
CC   -!- SIMILARITY: Belongs to the LptE lipoprotein family. {ECO:0000256|HAMAP-
CC       Rule:MF_01186}.
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DR   EMBL; CP000961; ACA87963.1; -; Genomic_DNA.
DR   RefSeq; WP_012326295.1; NC_010506.1.
DR   AlphaFoldDB; B1KDW1; -.
DR   STRING; 392500.Swoo_3703; -.
DR   KEGG; swd:Swoo_3703; -.
DR   eggNOG; COG2980; Bacteria.
DR   HOGENOM; CLU_103309_1_0_6; -.
DR   Proteomes; UP000002168; 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   Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR   HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR   InterPro; IPR007485; LPS_assembly_LptE.
DR   PANTHER; PTHR38098; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR   PANTHER; PTHR38098:SF1; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR   Pfam; PF04390; LptE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01186};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_01186, ECO:0000313|EMBL:ACA87963.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01186};
KW   Palmitate {ECO:0000256|HAMAP-Rule:MF_01186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01186}.
SQ   SEQUENCE   164 AA;  18825 MW;  C7F50B80B58B3EBD CRC64;
     MLIKRICFAI MTLAILFSAG CGFKLQGSYS IPEQLRTLHL SSQDQYSELT RLVRERLRLH
     SITLAEDSDN VPTLQILHDS LDRSTLSLYP TGNVAEYELT YHVTFAVAFP DKESQRFDVD
     IHRDYLDDPR TALAKSREME MLLKEMRIQA ADQMIQTLAS IEVK
//
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