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
//