LPTD_ACISJ
ID LPTD_ACISJ Reviewed; 817 AA.
AC A1WD88;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 70.
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=Ajs_4112;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM44213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000539; ABM44213.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041836136.1; NC_008782.1.
DR AlphaFoldDB; A1WD88; -.
DR SMR; A1WD88; -.
DR STRING; 232721.Ajs_4112; -.
DR PRIDE; A1WD88; -.
DR EnsemblBacteria; ABM44213; ABM44213; Ajs_4112.
DR KEGG; ajs:Ajs_4112; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_0_0_4; -.
DR Proteomes; UP000000645; 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..45
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 46..817
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281583"
SQ SEQUENCE 817 AA; 92059 MW; 3227D4ED491CD302 CRC64;
MDRLPLPHAL HVPTHRPFAA PLPPRRLLAR LAALMLCGVP LAVLAQAQPS QDAAPAEPPP
ALRSSPRLQE VLPYGIRQQL PVFVRGDRVT GQPDIQATIE GNAELRRGDT VVHADRMQYD
VADDRARASG NVLINRAGNR YEGSQLDLRV EAFTGFFSDA RYRFLETAAH GQASRVDFLD
RDRSVVHNAT YTTCERTDEA SWQPDWILRA ERIHLDRVED VGTAENGVLE FKGVPVLPIP
RITFPLSDRR KSGLLPPTLG LDSVSGFEYA QPYYWNIAPN RDATITPTVM TRRGVALGTE
FRYLEPRYSG ELTADYMPND RLRDRDRWAY GIKHRATFDT PAGGVGLGID IKRVSDDNYW
RDFSQRNSGR SGVNDQLTQR LLPGDATLNW ARGEHSLLLR TLKWQTLQDV NAPIIPPYDR
MPQLRWEYRP LQLAGGLDAS VEADYTSFHA DRAYTGQPNA KRSYTMAQVS RPFLAPAGFI
TPRVQLHSTH YEFDAPLANG QRTASRTLPT FSLDSGLVFE RDARYFGRDF LQTLEPRAFY
TYTPYRDQRL LPIYDTAVND FNFASIYTEN AFGGQDRLAD NNLLTLGVTT RLLDPDTGAE
AARFGVAQRV RFSDQEVTMP GGSPVNERLS DVLLGAGINW TPQWGFDSTV QYNPKTGRSL
RTTVGARYSP GNYRTVSAAY RMQKVTGLIT EPSEQIDVGW QWPLNDLWGD RGDKPSSAGG
RWYSVGRLNY SLQDRKLVDT VVGLEYESCC WIGRVVLERL QRSVTSSNTR LMFQIEFIGF
SRLSLGSNPL SSLKQNVPRY QFLRESVSTP SRFTQYD
