LPTD_SHESR
ID LPTD_SHESR Reviewed; 765 AA.
AC Q0HS09;
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=Shewmr7_3112;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
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 chromosome 1 of Shewanella sp. MR-7.";
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; CP000444; ABI44096.1; -; Genomic_DNA.
DR RefSeq; WP_011621703.1; NC_008322.1.
DR AlphaFoldDB; Q0HS09; -.
DR SMR; Q0HS09; -.
DR EnsemblBacteria; ABI44096; ABI44096; Shewmr7_3112.
DR KEGG; shm:Shewmr7_3112; -.
DR HOGENOM; CLU_009039_2_0_6; -.
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..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 19..765
FT /note="LPS-assembly protein LptD"
FT /id="PRO_5000129121"
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