ID W9T620_9PSED Unreviewed; 201 AA.
AC W9T620;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN ORFNames=BAY1663_04764 {ECO:0000313|EMBL:EXF42826.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF42826.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF42826.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF42826.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF42826.1}.
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DR EMBL; AZSV01000125; EXF42826.1; -; Genomic_DNA.
DR RefSeq; WP_037044728.1; NZ_AZSV01000125.1.
DR AlphaFoldDB; W9T620; -.
DR STRING; 1439940.BAY1663_04764; -.
DR PATRIC; fig|1439940.3.peg.4736; -.
DR eggNOG; COG2980; Bacteria.
DR OrthoDB; 5612114at2; -.
DR Proteomes; UP000019475; Unassembled WGS sequence.
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:EXF42826.1};
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:UP000019475};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01186}.
FT REGION 167..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 22679 MW; 335F55E0B4D6A302 CRC64;
MIKRNLVVLG LSLLLSACGF QLRGTGDVEF GLKEIDLQAR NSYGETVQQL EALLESNDVR
VHPGAKYSLN LANEQTRQRT ASYTSSARSA EYELTSVLDY EFRGPQNLLL LEDSVEVQKV
YVHDSNNLIG SSQEGDQLRQ EMRREILQQL VMRIQRITPA QLDRLQQEAE TRARAEAEAL
DAARRAQEAQ PQQSPVQLPI Q
//
