LPTD_CUPMC
ID LPTD_CUPMC Reviewed; 824 AA.
AC Q1LRA4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Rmet_0436;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(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; CP000352; ABF07322.1; -; Genomic_DNA.
DR RefSeq; WP_011515310.1; NC_007973.1.
DR AlphaFoldDB; Q1LRA4; -.
DR SMR; Q1LRA4; -.
DR STRING; 266264.Rmet_0436; -.
DR EnsemblBacteria; ABF07322; ABF07322; Rmet_0436.
DR KEGG; rme:Rmet_0436; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_0_0_4; -.
DR OMA; DYSHLDW; -.
DR OrthoDB; 100018at2; -.
DR Proteomes; UP000002429; 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; IPR007543; LptD_C.
DR Pfam; PF04453; LptD; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Membrane; Reference proteome; Signal.
FT SIGNAL 1..48
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 49..824
FT /note="LPS-assembly protein LptD"
FT /id="PRO_5000118484"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91744 MW; 455B2DC58AA5187F CRC64;
MTEQRRSPHH PATRPPAPPG TSRRVRLPAS ALRPLVLAMA GLTVSAHAQY GATSAIPNID
LVEPVVTQTP EAPPPPAEGG DLVPRLTEPA TRTAPSGNTL NLSPSSTPSN PNAPAYVSGD
RVTGYSEKGV EMEGHAELRR DGGVIKGDRL TYDQDTDEAH ATGNVRLSKS GTLAVGPEAR
MRVQANEGYM LSPDYYFQQT GGSGSAERVD FLDPDRSTLK KATYTTCSPD NADWYFSARK
LDLDSDRQVG TAYGGVLNFF GVPIAGAPAF SFPLNGERRS GVLPPLFGYG SNSGADLTVP
YYFNLAPNRD LTIYPRILTS RGVQLGEDFR YVGDGYSGRI RGEFLPDDKK AGRNRWAYSI
QHYQSIIPGM TAYVNVSKVS DDKYPDDLTR SVSQSTLRQY TQEGGVIYAW QDWVFMARVQ
KFQTLLPSEP SYEREPQLNA KYNRYDFHGF DISLETDYTR FRIPLTSTGF QQPEGNRAFI
QPTISYPIIH PGWYVTPKFI FNAAQYNMDA GTNTTGASNT LNRAIPTVSL DSGMTFERDA
PGVSKLFGVK YTQTLEPRLF YVYTPFYDQS QFPLFDTVQS DFGYGQIFTE NPFTGNDRIA
DNNKLTLGLT TRLIESETGV ERFRGTIAQR VDFTGQRVQL NGTLPDAKPS YSDLLAATTI
QLFRGYYLDA GIQWNPDQDK VNYSNVALAY RPESRKLINF GYRYRRPTSV TDNTAIDQIE
MSGQWPITQR TYGIGRVAFD KSANQLVDAL AGFEYAADCW VGRFVYQRFR NTSNGYTGRV
FFQVEFRGLS KIGSNPLDML RLNVPGYEPV TARPVPTTPY DHYE