ID W0DTR6_9GAMM Unreviewed; 172 AA.
AC W0DTR6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN ORFNames=THITH_14055 {ECO:0000313|EMBL:AHF00256.1};
OS Thioalkalivibrio paradoxus ARh 1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=713585 {ECO:0000313|EMBL:AHF00256.1, ECO:0000313|Proteomes:UP000005289};
RN [1] {ECO:0000313|EMBL:AHF00256.1, ECO:0000313|Proteomes:UP000005289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARh 1 {ECO:0000313|EMBL:AHF00256.1,
RC ECO:0000313|Proteomes:UP000005289};
RG DOE Joint Genome Institute;
RA Muyzer G., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007029; AHF00256.1; -; Genomic_DNA.
DR RefSeq; WP_006747268.1; NZ_CP007029.1.
DR AlphaFoldDB; W0DTR6; -.
DR STRING; 713585.THITH_14055; -.
DR KEGG; tti:THITH_14055; -.
DR HOGENOM; CLU_103309_0_2_6; -.
DR OrthoDB; 7349153at2; -.
DR Proteomes; UP000005289; 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};
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:UP000005289};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01186}.
SQ SEQUENCE 172 AA; 18781 MW; A697EC14B346F6AC CRC64;
MNAARIWGVA LLVLVLAGCG FQLRGVPDWP DGLDPIRIEG LAVRDPLYLN LAQSLRAAGV
EVLPPGTAGA AELRVLSLHD DRRVLSVTGA ARISEYELVR QLEAELALPD VAERLPLGRL
EVSRVYVFDA ASVLGQSERE EELRLAMNRD LVRLLQLRVQ ALLAQTPSGE SR
//
