ID Q63QT7_BURPS Unreviewed; 183 AA.
AC Q63QT7;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN OrderedLocusNames=BPSL2937 {ECO:0000313|EMBL:CAH36947.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH36947.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH36947.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH36947.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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: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; BX571965; CAH36947.1; -; Genomic_DNA.
DR RefSeq; WP_004194132.1; NZ_CP009538.1.
DR RefSeq; YP_109531.1; NC_006350.1.
DR AlphaFoldDB; Q63QT7; -.
DR STRING; 272560.BPSL2937; -.
DR GeneID; 56593775; -.
DR KEGG; bps:BPSL2937; -.
DR PATRIC; fig|272560.51.peg.2343; -.
DR eggNOG; COG2980; Bacteria.
DR OMA; YADMQND; -.
DR Proteomes; UP000000605; Chromosome 1.
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:CAH36947.1};
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:UP000000605};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01186}.
SQ SEQUENCE 183 AA; 19946 MW; 599F0192CB208037 CRC64;
MIRRSFLMLV GSAVLLSACG FKLRGQQDYA FKRLYIAGAP PAAAARLTRL VEAGSDTKIV
KTPDEADVVL NLAESRGQGT LTLDRFGTVQ EYQLNYSLNY TLFGKDGTLL IPPSLIALNR
AMTYSAKYTN AKAQESEILF ADMQNDAIDQ LMRRLAIVRT LHPEPGEGVP AVAPRAPLPP
PPL
//