ID   A0A1H2DXG4_9PSED        Unreviewed;       895 AA.
AC   A0A1H2DXG4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05216296_0140 {ECO:0000313|EMBL:SDT87585.1};
OS   Pseudomonas pohangensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=364197 {ECO:0000313|EMBL:SDT87585.1, ECO:0000313|Proteomes:UP000243232};
RN   [1] {ECO:0000313|Proteomes:UP000243232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17875 {ECO:0000313|Proteomes:UP000243232};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with LptE, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01411}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptE and LptA. {ECO:0000256|HAMAP-
CC       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}.
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DR   EMBL; LT629785; SDT87585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2DXG4; -.
DR   STRING; 364197.SAMN05216296_0140; -.
DR   OrthoDB; 9760225at2; -.
DR   Proteomes; UP000243232; Chromosome i.
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|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW   Rule:MF_01411};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01411};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243232};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT   CHAIN           33..895
FT                   /note="LPS-assembly protein LptD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT                   /id="PRO_5009355773"
FT   DOMAIN          151..282
FT                   /note="Organic solvent tolerance-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03968"
FT   DOMAIN          396..803
FT                   /note="LptD C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04453"
FT   REGION          52..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  99469 MW;  505558C609F3FBE7 CRC64;
     MATKLPDFRR NLPLLVTSSL LLLPVAVGQA IAADQFDCKA SATGGWACTP TSANANLPPR
     PPAQQSMPAA ADGSAASGES SGVVAGTAIA GQSLKAGKGS VDFSRLDWVP RSQLTTAQLK
     EVGPYCSGDY IEPKRPGMND KTPMSQAPMF VSAKASRYAQ QEQVATLAGD VVLRQSNIQI
     EADEANLYQA ENRGELKGDV KLRSPGMLVV GDEAEIQLDT GAAQIDQAEY VLHEANARGG
     AKYVKRGEDA IIRLKDGTYT TCAPGNNAWQ VKGNNIKLDP ATGMGTATNA TLRIKDIPVF
     YTPYIQFPID DRRQSGFLAP TAGYSNSDGV TLITPYYFNL APNYDATLYP RIMSERGLMM
     SGEGRYLTQS SEGKISGSYL DDQDDENKGQ PKYEQTRYLA SWQHTQGLDE RLLGEVDYTD
     ISDPYYFQDL GTDLDVSSQT YVNQQGVLTW RGDSFTAGLN VQSYELASVT DITPYDRLPQ
     VTLDGILPYQ PGGLQLSYGT EYVSFQRDLD SYYFNGIASP DQKLTGLNRA SGDRSHAQPG
     ISLPMENSWG YLTPSAKYLY TNYSLDLDSR GQSTLASGVQ YDDNQNRNIE LYSLDSGLYF
     DRDTTLFGKS LRQTLEPRLY YLYVPYKDQD DLPIFDTSEP SFNYQSLFRE NRFVGKDRIG
     DSNQLSAGTT SSFVEDNGFQ RAQIGIGQAF YFEDRQVQMP GITTQDASVS PTALFGQYRM
     DRDWRVSSDY AYNSDISKTS SGNLMFHYQP EATPNKIFNA GYRYRNDAIV FNEDTNEYEA
     GNDDEYKIEQ SDVSMIWPVL PQWSAIARWQ FDFNQSRTLE AFGGFEYDSC CWKLRLVSRY
     WVQPDDYNLE TNQQGDHGVF LQIVLKGLGG IAGNQVDSFL DQGIQGYRER EDKAF
//