LPTD_SHISS
ID LPTD_SHISS Reviewed; 784 AA.
AC Q3Z5V5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-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=SSON_0062;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000038; AAZ86857.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z5V5; -.
DR SMR; Q3Z5V5; -.
DR EnsemblBacteria; AAZ86857; AAZ86857; SSON_0062.
DR KEGG; ssn:SSON_0062; -.
DR HOGENOM; CLU_009039_2_0_6; -.
DR OMA; DYSHLDW; -.
DR Proteomes; UP000002529; 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..784
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281638"
FT DISULFID 31..724
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT DISULFID 173..725
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
SQ SEQUENCE 784 AA; 89685 MW; BCBA80525D16DAB6 CRC64;
MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL PVTINADHAK
GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP VRTVDALGNV HYDDNQVILK
GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILDNGSF TSCLPGSDTW
SVVGSEIIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY
FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED
EHPNDDSSRR WLFYWQHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS TDGYATQKFS
VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ NDVGPFDTRI YGQAVHFVNT
RDDMPEATRV HLEPTINLPL SNNWGSINTE AKLLATHYQQ TNLDWYNSRN TTKLDESVNR
VMPQFKVDGK MVFERDMEML APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL
FRDRTYGGLD RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND
DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR LVQLNYRYAS
PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV GAYYYDTNAN KQADSMLGVQ
YSSCCYAIRV GYERKLNGWD NDKQHAVYDN AIGFNIELRG LSSNYGLGTQ EMLRSNILPY
QNTL
