ID   LPTD_SALCH              Reviewed;         786 AA.
AC   Q57TG7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=SCH_0088;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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   -!- PTM: Contains two intramolecular disulfide bonds. {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; AE017220; AAX63994.1; -; Genomic_DNA.
DR   RefSeq; WP_011264183.1; NC_006905.1.
DR   AlphaFoldDB; Q57TG7; -.
DR   SMR; Q57TG7; -.
DR   EnsemblBacteria; AAX63994; AAX63994; SCH_0088.
DR   KEGG; sec:SCH_0088; -.
DR   HOGENOM; CLU_009039_2_0_6; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000000538; 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; Disulfide bond; Membrane; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           25..786
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000020286"
FT   DISULFID        31..726
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   DISULFID        173..727
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
SQ   SEQUENCE   786 AA;  89843 MW;  FE7A1E7494B92EC5 CRC64;
     MKKRIPTLLA TMIASALYSH QGLAADLASQ CMLGVPSYDR PLVKGDTNDL PVTINADNAK
     GNYPNDAVFT GNVDIMQGNS RLQADEVQLH QKQAEGQPEP VRTVDALGNV HYDDNQVILK
     GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILENGSF TSCLPGSDTW
     SVVGSEVIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTKNY
     FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLT QAGAGLMELD YLPSDKVYED
     DHPKEGDKHR WLFYWQHSGV MDQVWRFNVD YTKVSDSSYF NDFDSKYGSS TDGYATQKFS
     VGYAVQNFDA TVSTKQFQVF NDQNTSSYSA EPQLDVNYYH NDLGPFDTRI YGQAVHFVNT
     KDNMPEATRV HLEPTINLPL SNRWGSLNTE AKLMATHYQQ TNLDSYNSDP NNKNKLEDSV
     NRVMPQFKVD GKLIFERDMA MLAPGYTQTL EPRVQYLYVP YRDQSGIYNY DSSLLQSDYN
     GLFRDRTYGG LDRIASANQV TTGVTTRIYD DAAVERFNVS VGQIYYFTES RTGDDNIKWE
     NDDKTGSLVW AGDTYWRISE RWGLRSGVQY DTRLDSVATS SSSLEYRRDQ DRLVQLNYRY
     ASPEYIQATL PSYYSTAEQY KNGINQVGAV ASWLIADRWS IVGAYYFDTN SSKPADQMLG
     LQYNSCCYAI RVGYERKLNG WDNDKQHAIY DNAIGFNIEL RGLSSNYGLG TQEMLRSNIL
     PYQSSM