ID   LPTD_ACIAC              Reviewed;         820 AA.
AC   A1TWF7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
GN   Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA;
GN   OrderedLocusNames=Aave_4764;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-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   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- CAUTION: No signal sequence is predicted for this protein. All LptD
CC       proteins in this family possess a predicted signal sequence and are
CC       located on the bacterial outer membrane. {ECO:0000305}.
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DR   EMBL; CP000512; ABM35295.1; -; Genomic_DNA.
DR   RefSeq; WP_011797761.1; NC_008752.1.
DR   AlphaFoldDB; A1TWF7; -.
DR   SMR; A1TWF7; -.
DR   STRING; 397945.Aave_4764; -.
DR   EnsemblBacteria; ABM35295; ABM35295; Aave_4764.
DR   KEGG; aav:Aave_4764; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_009039_0_0_4; -.
DR   OMA; YDRMPQI; -.
DR   OrthoDB; 100018at2; -.
DR   Proteomes; UP000002596; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-UniRule.
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   Reference proteome.
FT   CHAIN           1..820
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281582"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  91722 MW;  23FAE39F0F5F6810 CRC64;
     MDLSSLPDPL RPTHSRLPAR RRDRAEPPRF EQRALARLAA WMVCGLPLAA LAQTDPGPGA
     TAEPAPALRS SPLLQEKIPE DARPKLPIFV RGDHVSGQPD INATVEGNAE LRRGDTIIHA
     DRLDYAVPDD LAKARGNVRI NRAGNVYEGS VLELQVDAFS GFFDDASYRF LANGAYGDAR
     RVDFIDRDRA LVHEATYTTC QKNDESTWKP AWIVRARSIK IDNAEQVGTA EGGVLEFQGV
     PILPVPGSFT FPLSDKRKTG LLPPTVGIDS VSGVVYSQPY YWNIAPNRDA TITPMVMSKR
     GVSTSGEFRY LEPTYSGELR GDYMPSDRLR NRDRWALGLK HRGVFDTGIG GIGLNVDATR
     VSDDNYWRDF STRTNGGISQ LTQRLLPADA TLFWGANDMS LSLRTLKWQT LQDVNARIVP
     PYDRMPQIHW GYMPSSLPGG FDGSVEADYT DFRADRALTG QPNARRSYAM AQFSRPFLAP
     AGFITPRLQF HATQYDFDSA LPSTGRRTAS RVLPTFSLDS GLVFERDARY FGRNFLQTLE
     PRAFYTYTPF RDQSMIPVYD TAANDFNFAT IYTENGYSGS DRIADNNLLT LGVTTRLLDP
     EDGGEAARFG IAQRLRFSDQ KVVMPGEAPV SERLSDVLVG AGINWTRQWG FDSTVQYNPK
     TSRSIRSTIG ARYNPSDYRV INAAYRFQRG TSEQIDVGWQ WPINDLWGDK GQNLGPGRGQ
     GGGRWYSVGR LNYSLQDRKL VDTVIGFEYD SCCWIGRVVL ERLQSSVTTA TTRLLFQIEF
     VGFSRLSLGS DPIQTLKQNI PRYQYLREPV PPPSRFTNYD