ID   LPTD_SHESM              Reviewed;         765 AA.
AC   Q0HLS9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Shewmr4_0908;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP000446; ABI37988.1; -; Genomic_DNA.
DR   RefSeq; WP_011621703.1; NC_008321.1.
DR   AlphaFoldDB; Q0HLS9; -.
DR   SMR; Q0HLS9; -.
DR   KEGG; she:Shewmr4_0908; -.
DR   HOGENOM; CLU_009039_2_0_6; -.
DR   OMA; DYSHLDW; -.
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..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           19..765
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_5000129610"
SQ   SEQUENCE   765 AA;  87460 MW;  DDAEBD613E56EE35 CRC64;
     MQIRYFLALS LLPQLVLADE SPTASASQCV IEPPVPRIVS QPGLSAADQE KIRIVSDRSN
     AEMGKQAIFT GDVVFSQGDR HIAADEAILD QATEQFDANG NLVFQDNIFT VTADSLQAQM
     RSNRATLKGA QYWLHGQQVH GDAEKLQITM NNNLILTNTN FTTCPPDNVS WLLEAEKIKI
     NSEEEWGEIW NAKLRIADIP VFYIPYMTVP VSDKRKTGFL YPSFSTSTTN GFEVSAPYYW
     NIAPEYDLTF TPNYMSSRGL FTKTEFRYLA GEAQSGRLNL EYLGNDQMLS GSPNRYLYNW
     QHQGAIDKNW RVLANFTEVS DNNYFNDLKS DVNRATDNQL SRIGEVSYFE RNWDISTRVQ
     DIKVLGEDEK PYQVMPQVNF NYRAADFWNN LDFGFNSELT NFAHDDSDMN TATRLHMAPS
     LTLPIHGPSG SLTSQVKLMQ TNYWQEQNNS AFDGLDDTVS RTIPQVRING QINFERFTEL
     FDQNYRQTLE PQFQYLYVGY EDQRGIGIYD TAQLQDDYFG LFRDRRFSGL DRIADANQVT
     LGVTTRFFDD HNQEATKFSL GQILYLQDSK LGYEDNLFEQ NQSTSVLAAE LDTRLSHDWY
     LGAAIQYDTN SSNNKKTEVT LDFRPEANKL LQLSYRYVPD LLNSNTNDLV NISQAGVRGA
     WPINDSLYFV GNWYYDLNES RSIETYTGFQ YESCCYAIRL SYHYRIKTNY DDNIGSAVID
     EREQFESGVY LNLVIKGLGG SGPLGVSDML NDGLFNYRKP LYLRN