LPTD_PSEMY
ID LPTD_PSEMY Reviewed; 938 AA.
AC A4XZJ1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Pmen_4010;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP86757.1; -; Genomic_DNA.
DR RefSeq; WP_012019861.1; NC_009439.1.
DR AlphaFoldDB; A4XZJ1; -.
DR SMR; A4XZJ1; -.
DR STRING; 399739.Pmen_4010; -.
DR EnsemblBacteria; ABP86757; ABP86757; Pmen_4010.
DR KEGG; pmy:Pmen_4010; -.
DR PATRIC; fig|399739.8.peg.4062; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_1_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..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 34..938
FT /note="LPS-assembly protein LptD"
FT /id="PRO_5000240920"
FT REGION 52..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 106652 MW; C08E0F7201F9BD59 CRC64;
MAVKHPAFRK KFPLLVTGSL LALQPAFSLQ SFAAEQYDCQ ASPTGGWACA PKTATSALPP
RPQHSRSAVS TTSGSATATA TKQEPAPVLV TESKGRALAS RSPDYSHLDW VPRDKLTAAQ
LAEAGPYCAG AYIEPLRPGM DDTTPLDESP MYVSAKASRY EQEKQIATLA GDVVLRQSGM
QVEADEASLH QAENRGELVG NVRLRDKGTL VVGDRAELQL DNGEARIDNA EYVMHQAHVR
GSALYAKREE TAIIRLKDGT YTRCEPGDNA WHLKGNNVTL NPATGFGTAT NVTLRVKDIP
VFYTPYIYFP IDDRRQSGFL PPSLGTSSSN GFSLQTPYYF NLAPNYDATL YPTYMAKRGL
LMEGEFRYLT ESSEGQVGGA WLNDQEDERK LQSEYEDQRW MYSWQHKQGL NSRLLAEVDY
TDISDPYYFQ DLDTDLGIET QSYVNQRGTL TYRGDSYTAR LNVHAYELAN ITDITPYDRL
PQITLDGKLP FNPGGLDFTY GTEYVRFDRN LRSGFFVDKD GVTGRPQDLW YDARLTGLNR
ADGERLHLEP GVSLPLNWSW GFVKPQVKYL HTQYQVNLDG QGKADLATND PENQWFGVDY
KGSPNRGVGL FSLDSGLYFD RNTQLFGRET RQTLEPRAFY LYVPEEDQTD IPIFDTGEPT
FSYASLWREN RFSGKDRIGD ENKLSLGVTS RWIEPNGFER QRFSVGQAFY FEDRKVQLAG
IDYRGRQDAT SDVSPYALEY LYRFNRDWRF SSTFNWDPDQ HATRSGSAMF HYQPEDNPNK
IVNLGYRYRN DIVRYDRDSG TWTTNPDYGN PTLADGSPNP NYIKNYYKID QHDFSVIWPL
APQWSLISRW QYDYGRNRTL EAFGGFEYDS CCWKLRLINR YWIDYDEVSL DPSRNDEPDR
GIFLQIVLKG LGGVVGNKVE TFLDQGIQGY REREDQAF