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Database: UniProt
Entry: J9DXT3_9PROT
LinkDB: J9DXT3_9PROT
Original site: J9DXT3_9PROT 
ID   J9DXT3_9PROT            Unreviewed;       706 AA.
AC   J9DXT3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=LPS-assembly protein LptD {ECO:0000256|HAMAP-Rule:MF_01411};
DE   Flags: Precursor;
GN   Name=lptD {ECO:0000256|HAMAP-Rule:MF_01411};
GN   ORFNames=IMCC14465_02510 {ECO:0000313|EMBL:EJW21857.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW21857.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW21857.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW21857.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT   to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(2012).
CC   -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS) at the
CC       surface of the outer membrane. {ECO:0000256|HAMAP-Rule:MF_01411}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. {ECO:0000256|HAMAP-Rule:MF_01411}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01411}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01411}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW21857.1}.
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DR   EMBL; ALYF01000002; EJW21857.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9DXT3; -.
DR   STRING; 1220535.IMCC14465_02510; -.
DR   eggNOG; COG1452; Bacteria.
DR   Proteomes; UP000004836; 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   Gene3D; 2.60.450.10; Lipopolysaccharide (LPS) transport protein A like domain; 1.
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   PANTHER; PTHR30189; LPS-ASSEMBLY PROTEIN; 1.
DR   PANTHER; PTHR30189:SF1; LPS-ASSEMBLY PROTEIN LPTD; 1.
DR   Pfam; PF04453; LptD; 1.
DR   Pfam; PF03968; LptD_N; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01411};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01411};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004836};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT   CHAIN           23..706
FT                   /note="LPS-assembly protein LptD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT                   /id="PRO_5009015747"
FT   DOMAIN          32..122
FT                   /note="Organic solvent tolerance-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03968"
FT   DOMAIN          282..641
FT                   /note="LptD C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04453"
SQ   SEQUENCE   706 AA;  79327 MW;  417F014E5EECA39C CRC64;
     MRSIFLAGFI MCLCMTPLQV KAQNQNDNQA LIEADSMSFE QDTEIVSASG NVTIQYRGRE
     LRADTITWDQ KSDRIIASDN VILIDTDGTR VTTQSAELRD EMKQATLKKF SLMMKNNLSF
     KGETASRQAG KSTKISKAIF TACKPCKNNP NAAPTWQLRS GETIYDETGE TIFHKNVRLE
     MRGVPVFYFP YLVHPAPDVK KRSGFLFPDI KSSTDTGADI ALPYFINLAP DYDLTLTPRL
     IANGGSMLGF DWRQKIPQGT YSIAGNGLWV DEDKNVDNDK TFRGNIEGKG VFKLNENWRA
     GFNYWWLSDK SFMRRYDIND ADYFTSQAYL RKTSGRNIID VRLLDFKTSI VDIDEDAQPE
     VAPQIRTAHY FENLAGGDLR LSSDFLSLSR KNGTDVTRAV AETEWTRQSI LKSGQILDYF
     GGIRGAYHDY EIDNNGQNLS DNSAVVLGHA GAKWRMPFIK RQAAGAVIIE PTAQVIIANE
     ETSQSSIPNE DSPSTEFDSL NIFDVYRHTG FDRFDTGNRL DVGVNTLFEA DNGSSYSMFV
     GKSYRDKATT QPTIGTKSGK KASDWLLDFD LQQASGFGFN GQLRFDDDNQ RLIRSDGEIS
     ASIKQAHFAL RYTHLDASIT SDGSDREEAR GSLDINLSEN WRLNSYVRYD VEREQRLKNS
     IGLTYRDDCT DISLTFNQSF TQNGNIGPRN GIAFKIILRT LGGSNR
//
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