ID A0A3N5CU08_9SPHN Unreviewed; 780 AA.
AC A0A3N5CU08;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=EG799_04140 {ECO:0000313|EMBL:RPF70900.1};
OS Aurantiacibacter spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2488860 {ECO:0000313|EMBL:RPF70900.1, ECO:0000313|Proteomes:UP000275232};
RN [1] {ECO:0000313|EMBL:RPF70900.1, ECO:0000313|Proteomes:UP000275232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E23 {ECO:0000313|EMBL:RPF70900.1,
RC ECO:0000313|Proteomes:UP000275232};
RA Zhuang L., Luo L.;
RT "Erythrobacter spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPF70900.1}.
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DR EMBL; RPFZ01000001; RPF70900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5CU08; -.
DR OrthoDB; 9760225at2; -.
DR Proteomes; UP000275232; 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 PANTHER; PTHR30189; LPS-ASSEMBLY PROTEIN; 1.
DR PANTHER; PTHR30189:SF1; LPS-ASSEMBLY PROTEIN LPTD; 1.
DR Pfam; PF04453; LptD; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01411};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01411};
KW Reference proteome {ECO:0000313|Proteomes:UP000275232};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT CHAIN 36..780
FT /note="LPS-assembly protein LptD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT /id="PRO_5018341215"
FT DOMAIN 340..706
FT /note="LptD C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04453"
SQ SEQUENCE 780 AA; 86314 MW; 486A6F96DF4BF5D4 CRC64;
MPIGQPFAPQ AVPLRLPLAG IVAALLLGLP CSVLAQAGAA PGVDTAQDNP VEDDILDARL
PDDGSVPAPP VLPQFNAAGE RQIAFEANEL EYDSTTETVT ASGNVFIRSG DQSVRADAVT
WNRLTGEIVA TGDIRFVDED GNQLFTDRLV LTDELEAGAM DNLLLVFQEG GRLAAEQARR
DEAGDIALTR AAYSSCAVET GSGCPKRPSW RLTAERVTYD SATDKIRFRD AYLELFGARV
LPLPGLTIRA GGGANSGIFI PDVGITASNG IEISDSYYMR LADNRDLTLS AYVYTEAAPM
ASAQYRHLTG NGAFQVTGYI THGSRIPLGS QRLISEDGLR GYVFSNGRFQ IGEHWTATGS
LRIASDRTFL RRYDISREDR IRSMVELERI DDRSYLSLSG WATQALLVDT PQGQVPLALP
LIDARYLLDD PVLGGDIELQ ANTLAVTRGD GQDTQRAFAR AQWDLRRITR WGQEVTFTAL
ARGDIYHSDG NALNPVPLYS GQPGWQGRAV AIGALDVKWP LIGSAFGGTQ TLTPRVQLVA
APDIRNLAIP NEDARAIDLE DSNLFALNRF PGYDRVEDGV RLTYGIDWEV NRPGWRVETT
VGQSYRLSDE PNLFPDGTGL NEQFSDFVGR TKIRYRDFIQ FTHRFRLDKD SFAVRRNEVD
ATVGSARTYA EIGYLRLNRD IDPLFQDLQD REELRLAGRL AFQRYWSVFG SAVVNLTDRE
EDPTFSADGF EPLRTRLGVA YADDCLEFGV TWRRDYIQLA DAQNGNSFRI YFRLRNLGFR
//