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Database: UniProt
Entry: A0A098U9C8_9BURK
LinkDB: A0A098U9C8_9BURK
Original site: A0A098U9C8_9BURK 
ID   A0A098U9C8_9BURK        Unreviewed;       170 AA.
AC   A0A098U9C8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN   Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN   ORFNames=IA69_14610 {ECO:0000313|EMBL:KGF81006.1};
OS   Massilia sp. JS1662.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF81006.1, ECO:0000313|Proteomes:UP000029701};
RN   [1] {ECO:0000313|EMBL:KGF81006.1, ECO:0000313|Proteomes:UP000029701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1662 {ECO:0000313|EMBL:KGF81006.1,
RC   ECO:0000313|Proteomes:UP000029701};
RA   Fida T.T., Spain J.C.;
RT   "Identification of Arachidin-3 degrading bacteria in the peanut
RT   rhizosphere.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with LptD, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane. Required
CC       for the proper assembly of LptD. Binds LPS and may serve as the LPS
CC       recognition site at the outer membrane. {ECO:0000256|HAMAP-
CC       Rule:MF_01186}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptD. {ECO:0000256|HAMAP-Rule:MF_01186}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01186}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_01186}.
CC   -!- SIMILARITY: Belongs to the LptE lipoprotein family. {ECO:0000256|HAMAP-
CC       Rule:MF_01186}.
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:KGF81006.1}.
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DR   EMBL; JPQD01000014; KGF81006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A098U9C8; -.
DR   Proteomes; UP000029701; 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   Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR   HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR   InterPro; IPR007485; LPS_assembly_LptE.
DR   PANTHER; PTHR38098; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR   PANTHER; PTHR38098:SF1; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR   Pfam; PF04390; LptE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01186};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_01186, ECO:0000313|EMBL:KGF81006.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01186};
KW   Palmitate {ECO:0000256|HAMAP-Rule:MF_01186};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01186, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..170
FT                   /note="LPS-assembly lipoprotein LptE"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008824419"
SQ   SEQUENCE   170 AA;  18702 MW;  2C92ADA460F1329B CRC64;
     MTRKLAVRAV AALLVASATA GCGFQLRGSN GSYTMPFHSI YLGFPDTSAL GTELKRNLRA
     TDQVVIADKA ADAEAQFVLL GESRNKSILS LNSLGRVREY LLTYTMSFTV RDAKGVELVP
     PTQISLRRNM AFDETQVLAK ESEEALLYRD MQADLVQQIM RRLASIKPAT
//
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