LPTD_CUPPJ
ID LPTD_CUPPJ Reviewed; 810 AA.
AC Q475Q4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=Reut_A0497;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ59879.1; -; Genomic_DNA.
DR RefSeq; WP_011296686.1; NC_007347.1.
DR AlphaFoldDB; Q475Q4; -.
DR SMR; Q475Q4; -.
DR STRING; 264198.Reut_A0497; -.
DR EnsemblBacteria; AAZ59879; AAZ59879; Reut_A0497.
DR KEGG; reu:Reut_A0497; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_0_0_4; -.
DR OMA; DYSHLDW; -.
DR OrthoDB; 100018at2; -.
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 InterPro; IPR005653; OstA-like_N.
DR Pfam; PF04453; LptD; 1.
DR Pfam; PF03968; LptD_N; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Membrane; Signal.
FT SIGNAL 1..49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 50..810
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281631"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 90726 MW; C5F5E5B54C069579 CRC64;
MTEQRRSPNK RANKPPALSG LSSRTGRLPA SALRPLVLAM AGLSVGAHAQ MSSSAVPDID
QTESVVETAP EVPLAPPVSG ELVPRLAEPA KTTQPGESPP AFVSGDRLTG YNERGVVLEG
NAELRRGGAV VKGDKLTYDQ DTDEAFAHGN ARVSRGGALA VGPEARMKVE ANEGYMLSPD
YYFQQTGGTG KAERIDFIDK DRSVIKRATY TTCSPDNADW YFSARQLDLD SDREVGVAYG
GVLHFFDVPI AGAPVFSFPL TDERRSGFLS PLFGYGSKSG LDVTLPYYFN IAPNRDLTLY
PRIMTSRGFM LGGDYRYIGQ GYSGRLRAEI LPDDRQTNSN RWSYSFQHTQ NLAKGLNAYL
NLNRVSDDRY PDDLTRTVAQ STQRQYIQEG GVTYNWQDFT VLARVQKFQT LLPSGPSYER
EPQLNGKYIR YDLGGFDVQV EADYTRFRIP LTSTGFQQPQ GERMFVQPTI SYPIVRPGWY
ATPKVIFNAT QYQMEPQSNT PTAQNNFSRT VPTFSFDSGM TFERDAPTMS RVFGVNYLQT
LEPRLFYVYT PFRDQSQFPL FDTVQSDFGY GQIFSENPFT GYDRVADNNK LTAGLTTRLI
EADTGIERFR GTIAQRYDFS GQRVQINGTL PDPKAGSSDL LAATTIQLFR GYYLDAGIQY
NPDSEHINYS NLAFAWRPEP RKLLNVGYRY RRATSVTDNT AIDQFEISGQ WPITQRAYGI
GRFAFDRNAN QMVDALAGLE YAADCWVGRV VYQRYRNTTQ GYTGRIFLQV EFRGLSKIGS
NPLDILRLNV PGYEPVTAKP VPTTQFDHYE