LPTD_BORPA
ID LPTD_BORPA Reviewed; 790 AA.
AC Q7W4J4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=BPP3667;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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; BX640434; CAE38951.1; -; Genomic_DNA.
DR RefSeq; WP_003814429.1; NC_002928.3.
DR AlphaFoldDB; Q7W4J4; -.
DR SMR; Q7W4J4; -.
DR EnsemblBacteria; CAE38951; CAE38951; BPP3667.
DR KEGG; bpa:BPP3667; -.
DR HOGENOM; CLU_009039_0_0_4; -.
DR OMA; DYSHLDW; -.
DR Proteomes; UP000001421; 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; 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_0000281590"
SQ SEQUENCE 790 AA; 88618 MW; 19A290F408949394 CRC64;
MRMLRWLILS AFSVAGAVQA QGNQDSAAAS ASSASIGAPV 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 QRPLLNGRRL
GPDGDRLQTY PTVSYPIVRP GWFLVPKVGV HYTQYRTDWY NRDWNRIGLS NYKRTESRTV
PIMSLDAGMI FERDASLFGK AATQTLEPRL YYLRVPYRDQ SALPVYDTTL ADFSFDQAFQ
ENIYTGGWDR IANANQLTAA LTTRWLDANT GFERLSLSAA QRIYFQDQEV TLPAEQPRKN
VRSDFLVGAT AALTDTLTTD VAAQYNPYDN KWSRGMVSAR WSPQRLTTVA VAYRYQRDPL
PGISYQPQGQ NQVSLAVQWP IHRRWYGVGR VDYSLRSEPA TAAAAEQSPR VTQAIAGLEY
KGDCCWVGRV VYQRYAVSAA DTNTALFFQL ELTGLGALGT DPISLLNRSI PGYQSVVPPT
PTGTTFERYE