ID   LPTD_NEIMH              Reviewed;         802 AA.
AC   F0MIT7; E6MWH0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE   AltName: Full=Organic solvent tolerance protein;
DE   Flags: Precursor;
GN   Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=ostA;
GN   OrderedLocusNames=NMBH4476_0275; ORFNames=NMH_1010;
OS   Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=909420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76;
RA   Piet J.R., Huis in 't Veld R., van Schaik B., van Kampen A., Baas F.,
RA   van de Beek D., Pannekoek Y., van der Ende A.;
RT   "Genome Sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76;
RX   PubMed=21368196; DOI=10.1073/pnas.1019751108;
RA   Budroni S., Siena E., Hotopp J.C., Seib K.L., Serruto D., Nofroni C.,
RA   Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A.,
RA   Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.;
RT   "Neisseria meningitidis is structured in clades associated with restriction
RT   modification systems that modulate homologous recombination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=H44/76;
RX   PubMed=15192148; DOI=10.1073/pnas.0402340101;
RA   Bos M.P., Tefsen B., Geurtsen J., Tommassen J.;
RT   "Identification of an outer membrane protein required for the transport of
RT   lipopolysaccharide to the bacterial cell surface.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9417-9422(2004).
CC   -!- FUNCTION: Together with LptE, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane.
CC       Determines N-hexane tolerance and is involved in outer membrane
CC       permeability. Essential for envelope biogenesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01411, ECO:0000269|PubMed:15192148}.
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, ECO:0000269|PubMed:15192148}.
CC   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADY94939.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AEQZ01000016; EFV64164.1; -; Genomic_DNA.
DR   EMBL; CP002420; ADY94939.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002243965.1; NC_017516.1.
DR   AlphaFoldDB; F0MIT7; -.
DR   SMR; F0MIT7; -.
DR   EnsemblBacteria; EFV64164; EFV64164; NMH_1010.
DR   KEGG; nmh:NMBH4476_0275; -.
DR   PATRIC; fig|909420.3.peg.350; -.
DR   HOGENOM; CLU_009039_0_0_4; -.
DR   Proteomes; UP000032707; Unassembled WGS sequence.
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   Pfam; PF04453; LptD; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           26..802
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000411118"
SQ   SEQUENCE   802 AA;  88693 MW;  3960E1F1C804B3AF CRC64;
     MARLFSLKPL VLALGLCFGT HCAAADAVAA EETDNPTAGE SVRSVSEPIQ PTSLSLGSTC
     LFCSNESGSP ERTEAAVQGS GEASIPEDYT RIVADRMEGQ SQVQVRAEGN VVVERNRTTL
     NTDWADYDQS GDTVTAGDRF ALQQDGTLIR GETLTYNLEQ QTGEAHNVRM EIEQGGRRLQ
     SVSRTAEMLG EGHYKLTETQ FNTCSAGDAG WYVKAASVEA DREKGIGVAK HAAFVFGGVP
     IFYTPWADFP LDGNRKSGLL VPSLSAGSDG VSLSVPYYFN LAPNLDATFA PSVIGERGAV
     FDGQVRYLRP DYAGQSDLTW LPHDKKSGRN NRYQAKWQHR HDISDTLQAG VDFNQVSDSG
     YYRDFYGNKE IAGNVNLNRR VWLDYGGRAA GGSLNAGLSV LKYQTLANQS GYKDKPYALM
     PRLSVEWRKN TGRAQIGVSA QFTRFSHDSR QDGSRLVVYP DIKWDFSNSW GYVRPKLGLH
     ATYYSLNRFG SQEARRVSRT LPIVNIDSGA TFERNTRMFG GEVLQTLEPR LFYNYIPAKS
     QNDLPNFDSS ESSFGYGQLF RENLYYGNDR INTANSLSAA VQSRILDGAT GEERFRAGIG
     QKFYFKDDAV MLDGSVGKKP RNRSDWVAFA SGSIGSRFIL DSSIHYNQND KRAENYAVGA
     SYRPAQGKVL NARYKYGRNE KIYLKSDGSY FYDKLSQLDL SAQWPLTRNL SAVVRYNYGF
     EAKKPIEVLA GAEYKSSCGC WGAGVYAQRY VTGENTYKNA VFFSLQLKDL SSVGRNPADR
     MDVAVPGYIT AHSLSAGRNK RP