ID   LPTD_BORPE              Reviewed;         790 AA.
AC   Q7VU13;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=BP3329;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640421; CAE43594.1; -; Genomic_DNA.
DR   RefSeq; NP_881865.1; NC_002929.2.
DR   RefSeq; WP_010931411.1; NZ_CP039021.1.
DR   AlphaFoldDB; Q7VU13; -.
DR   SMR; Q7VU13; -.
DR   STRING; 257313.BP3329; -.
DR   GeneID; 45387434; -.
DR   KEGG; bpe:BP3329; -.
DR   PATRIC; fig|257313.5.peg.3608; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_009039_0_0_4; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000002676; 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   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; IPR045659; LptD_2.
DR   InterPro; IPR007543; LptD_C.
DR   Pfam; PF04453; LptD; 1.
DR   Pfam; PF19838; LptD_2; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           21..790
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281591"
SQ   SEQUENCE   790 AA;  88588 MW;  50F43CE3107CB9D2 CRC64;
     MRMLRWLILS AFSVAGAVQA QGNQDSAAAS APSASIGAPV LRTSPGLRVH RLPDEKIPAF
     MEADQISGDP DSEVTLTGNA QVRRVDGIIK GDRINYRRDT GDVDVQGSAR MLRDGTLITG
     PSARLNVDTY SGEIQEPNFW IGASGGTAQA RHADIFSKSQ MRLSQVTYSG CPCPKPSWYI
     KADTVDLDFD ENEGVARNGV LYFKDVPILA SPYLTFPVKK ERKSGFLMPT YGTTSNSGFD
     ISLPYYFNLA PNYDLTLVPR YLSKRGAQLG GEFRYLGSGY RGVAIGTYLP DDNETGRDRW
     MYRTYHRQLL GNGFYTDWDI AGASDDNYFR DISELGLNTA STTYLPRRGR VGWSSTYWQT
     YAQVYKYQTL QDPDAPLAPP YDKVPELWLK GARYDWGGFD AEWVSTAVRF QRSLLNGRRL
     GPDGDRLQTY PTVSYPIGRP GWFLVPKVGV HYTQYRTDWY NRDWNRIGLS NYKRTESRTV
     PIMSLDAGMI FERDASLFGK AATQTLEPRL YYLRVPYRDQ SALPVYDTTL ADFSFDQAFQ
     ENIYTGGWDR IANANQLTAA LTTRWLDANT GFERLSLSAA QRIYFQDQEV TLPAEQPRKN
     VRSDFLVGAT AALTDTLITD VAAQYNPYDN KWSRGMVSAR WSPQRLTTVA VAYRYQRDPL
     PGISYQPQGQ NQVSLAVQWP IHRRWYGVGR VDYSLRSEPA TAAAAEQSPR VTQAIAGLEY
     KGDCCWVGRV VYQRYAVSAA DTNTALFFQL ELTGLGALGT DPISLLNRSI PGYQSVVPPT
     PTGTTFERYE