LPTD_BURPS
ID LPTD_BURPS Reviewed; 787 AA.
AC Q63X79;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE Flags: Precursor;
GN Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA;
GN OrderedLocusNames=BPSL0658;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., 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 LptE, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01411}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptE and LptA. {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
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DR EMBL; BX571965; CAH34651.1; -; Genomic_DNA.
DR RefSeq; WP_004189876.1; NZ_CP009538.1.
DR RefSeq; YP_107287.1; NC_006350.1.
DR AlphaFoldDB; Q63X79; -.
DR SMR; Q63X79; -.
DR STRING; 272560.BPSL0658; -.
DR EnsemblBacteria; CAH34651; CAH34651; BPSL0658.
DR GeneID; 56596647; -.
DR KEGG; bps:BPSL0658; -.
DR PATRIC; fig|272560.51.peg.962; -.
DR eggNOG; COG1452; Bacteria.
DR OMA; DYSHLDW; -.
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 GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro.
DR GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR InterPro; IPR020889; LipoPS_assembly_LptD.
DR InterPro; IPR007543; LptD_C.
DR Pfam; PF04453; LptD; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Membrane; Reference proteome; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 40..787
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281593"
SQ SEQUENCE 787 AA; 86453 MW; 41955832D4CB01EA CRC64;
MPPKTLFPLV PACDAAPRKK RLAVALLAVP GLVPAVSQAQ LSGAAAEPQA FGSPWDLRLA
PQLDEHPQKQ GGKPATFVLA DHTNGTAEQD LAAKGAAEIR RGNAAVKADA IHYDQDTDMA
DAYGKVTVAN GGTTFSGPEA HLKVEANQGF MTTPKYRFTA TGGTGSAERV QLLDSERSVF
TNGTYTGCQC STNPAWYIKG SEFDFDTGAD EGVARNGVLF FQGVPLFGSP WLTFPLSGDR
RSGFLPPTFS PFSSTNGFEL SLPYYFNIAP NRDLTITPHI ISKRGIFTQA TFRYLSTNYS
GTLTGEYLPD DRVAHRNRYA IFWQHQQNFG NGFGGYVYYN KVSDNLYPEE LGSTNQFVNG
VQTVYQQEAG LTYNNGPWSV LGRYQHWQTL PPSAAPYGRE PQLNVKYTKY NVGGFDFGAE
ADYSRFRITT ADQPEGDRVM FNPYVSYGLY GPGYFFVPKA QLHMASYDLT TTTGGVPGQP
KRFTYSIPTL SLDTGLVFDR SVRLFGQDFI QTLEPRLFYV YTPYRNQSNA PLFDTAVSDF
GLAEIFTPNT FVGNDRIADA NRLTAALTTR FINPTTGDER ARFVIAQQYY FTDQRVTLLP
TEAPATARHS DLILGASVKL GAGFASETAF QYNVDNNQLV KSSVGFGYSP GERRVINVGY
RYTRQNPTLS NEPINQILMS AQWPLTRRLY AVGRLNYDLA SSRVVDGLVG FQYDADCWAF
GVGVQRYANG LNSSGQQNSS TRVLAQLVLK GLTSIDNGLV TAFRAGVQGY TPLPPAPAPL
SRFSNYD