LPTD_SALTY
ID LPTD_SALTY Reviewed; 786 AA.
AC Q8ZRW0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=STM0093;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- INTERACTION:
CC Q8ZRW0; Q8ZQZ7: lptE; NbExp=3; IntAct=EBI-16111554, EBI-16111540;
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; AE006468; AAL19057.1; -; Genomic_DNA.
DR RefSeq; NP_459098.1; NC_003197.2.
DR RefSeq; WP_000746127.1; NC_003197.2.
DR PDB; 4N4R; X-ray; 2.80 A; A/C=1-786.
DR PDBsum; 4N4R; -.
DR AlphaFoldDB; Q8ZRW0; -.
DR SMR; Q8ZRW0; -.
DR DIP; DIP-61032N; -.
DR IntAct; Q8ZRW0; 1.
DR STRING; 99287.STM0093; -.
DR PaxDb; Q8ZRW0; -.
DR EnsemblBacteria; AAL19057; AAL19057; STM0093.
DR GeneID; 1251611; -.
DR KEGG; stm:STM0093; -.
DR PATRIC; fig|99287.12.peg.96; -.
DR HOGENOM; CLU_009039_2_0_6; -.
DR OMA; DYSHLDW; -.
DR PhylomeDB; Q8ZRW0; -.
DR BioCyc; SENT99287:STM0093-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
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 DisProt; DP02518; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Membrane;
KW Reference proteome; 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_0000020289"
FT DISULFID 31..726
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT DISULFID 173..727
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 269..280
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 325..336
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 356..365
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 388..400
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 407..424
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 426..442
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 445..457
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 481..493
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 507..519
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 540..543
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 557..569
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 575..588
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 605..616
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 619..631
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 634..649
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 652..661
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 663..669
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 678..682
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 684..693
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 700..708
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 709..712
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 713..722
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 731..742
FT /evidence="ECO:0007829|PDB:4N4R"
FT TURN 743..746
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 747..751
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:4N4R"
FT HELIX 772..775
FT /evidence="ECO:0007829|PDB:4N4R"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:4N4R"
SQ SEQUENCE 786 AA; 89872 MW; 190AA418CB852237 CRC64;
MKKRIPTLLA TMIASALYSH QGLAADLASQ CMLGVPSYDR PLVKGDTNDL PVTINADNAK
GNYPDDAVFT GNVDIMQGNS RLQADEVQLH QKQAEGQPEP VRTVDALGNV HYDDNQVILK
GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILENGSF TSCLPGSDTW
SVVGSEVIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTKNY
FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLT QAGEGVMELD 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 ASWPIADRWS IVGAYYFDTN SSKPADQMLG
LQYNSCCYAI RVGYERKLNG WDNDKQHAIY DNAIGFNIEL RGLSSNYGLG TQEMLRSNIL
PYQSSM
