ID   LPTD_XANC5              Reviewed;         809 AA.
AC   Q3BX79;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=XCV0903;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ22534.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3BX79; -.
DR   SMR; Q3BX79; -.
DR   STRING; 456327.BJD11_18275; -.
DR   EnsemblBacteria; CAJ22534; CAJ22534; XCV0903.
DR   KEGG; xcv:XCV0903; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_009039_0_0_6; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000007069; Chromosome.
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..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           23..809
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_5000075439"
SQ   SEQUENCE   809 AA;  91833 MW;  40A313ED3B1E3586 CRC64;
     MRRALRLLPL PLSIAICLPA MAADKPLNWG LCPAVDPLPG FDGAPAADPK AAEMRQQLPT
     DIEGDQLSGT STTPQYQGNV ALKRGDQFLG ADNLRMDTET GNYIAEGNVR YQDTSFRMVA
     DRAEGNQDTD THKVTNIQYQ LVERRGNGDA ESVDLQGQVG QMHRSTYTTC DPSQPIWRVR
     APEIDVDNEE GFGTARNAVL QIGKVPVLYF PWFKFPIDDR RQTGLLFPQF GLSGRNGFDY
     LQPIYLNLAP NYDATLLPRY MSKRGFMFGT EFRYLYEGGR GEVTGNYLPN DKLRDKDRGS
     VFYSGYHNVN SNWQARSSIS WVSDTRYVED FTSRINGMGS ASSLQSTVGI YGTGETWTAG
     LMADRWQLTD YTLDEQALPY NRQPRAYFTW EKPLGIFEAG IYAEAVRFTH DDSYFVRPPI
     SGSSRDDNED EYVRTNIRNK QYGSGARLDV KPYISMPLSG AAWFLTPTVA WRYTAYQLDS
     TLADTAPLTG NRTPTRSLPI ASLDAGLYFD RETSLFGTNY LNTLEPRMYY LYVPYRDQDD
     LPVFDTRPFT FSYGQLFRDT RYTGADRQND ANQLTLAVTS RWLRQDDGRE KLSLSAGQIL
     YFSDSLVTIN NSNNSAAGSE QTVEQGKSAW VADANYMIND RWSMGATYQW NPNSRKEDLA
     SLRTRYLLNN DGIINLAYRY RRNLTDNSDQ LKQADFSFLY PINPSWSAVG RYYYSLLDRK
     PLEIIGGVQW DSCCLAVRGL VRRFVRNRDG EMDNSIQIEF VLKGLSSFGQ NTDRTLRRAI
     LGYYRDDLYL VPPSNTTTNP DDYDPNLIP