LPTD_SHEON
ID LPTD_SHEON Reviewed; 765 AA.
AC Q8EB96;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SO_3636;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56622.1; -; Genomic_DNA.
DR RefSeq; NP_719178.1; NC_004347.2.
DR RefSeq; WP_011073439.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EB96; -.
DR SMR; Q8EB96; -.
DR STRING; 211586.SO_3636; -.
DR PaxDb; Q8EB96; -.
DR KEGG; son:SO_3636; -.
DR PATRIC; fig|211586.12.peg.3525; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_2_0_6; -.
DR OMA; DYSHLDW; -.
DR OrthoDB; 100018at2; -.
DR PhylomeDB; Q8EB96; -.
DR BioCyc; SONE211586:G1GMP-3387-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
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; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 19..765
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281633"
SQ SEQUENCE 765 AA; 87555 MW; 91F88DADF008FA74 CRC64;
MQIRYLLALS LLPKLVLADE SPATSASQCL IEPPVPRIVS QPGLSAADQA KIRIASDRSK
AEMGKQAIFT GDVVFSQGDR HIAADEAILD QATEQFDANG NLVFQDSNFT VTADSLQAQM
RSNRATLTGA QYWLHGQQVH GDAEKLQITI NNNLILTNTN FTTCPPDNVS WLLEAEKIKI
NSEEEWGEIW NAKLRVADIP VFYIPYMTVP VSDKRKTGFL YPSFSTSTTN GFEVSAPYYW
NIAPEYDLTF TPNYMTNRGL FTKTEFRYLA GEAQNGRLNL EYLGSDQMLN GSPNRYLYNW
QHQGAIDKNW RVLANFTEVS DNNYFNDLKS DVNRATDNQL SRIGEVSYFE RDWDISTRVQ
DIKVLGEDEK PYQVMPQVNF NYRAADFWNN LDFGFNSELT NFAHQDDDVN TATRLHMAPS
LTLPIHGPSG SFTSQLKLMQ TNYWQEKNNS KFDSLDDTVS RTIPQVRING QINFERFTEL
FEHNYRQTLE PQFQYLYVGY EDQRGIGIYD TAQLQDDYFG LFRDRRFSGL DRIADANQVT
LGITTRLFDD HNQEATKFSL GQIFYLQDSK LGYEDNIFEQ NQSTSVLAAE LDTRLSSNWY
LGAAIQYDTN TSDNKKTEVT LDFRPEANKL LQFSYRYVPD LLNSNTNDLV NISQAGVRGA
WPINDSLYFV GNWYYDLNET RSIETYTGVQ YESCCYAIRL SYHYRIKTNY DDNIGSTIID
EREQFESGVY LNLIIKGLGG SGPLGVSDML NDGLFNYRKP LYLRN