LPP_PROMI
ID LPP_PROMI Reviewed; 78 AA.
AC P09461;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Major outer membrane lipoprotein Lpp {ECO:0000255|HAMAP-Rule:MF_00843};
DE Flags: Precursor;
GN Name=lpp {ECO:0000255|HAMAP-Rule:MF_00843};
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007466; DOI=10.1016/s0021-9258(17)38544-7;
RA Ching G., Inouye M.;
RT "Expression of the Proteus mirabilis lipoprotein gene in Escherichia coli.
RT Existence of tandem promoters.";
RL J. Biol. Chem. 261:4600-4606(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3903165; DOI=10.1016/0022-2836(85)90066-x;
RA Ching G., Inouye M.;
RT "Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning and
RT DNA sequence of the lpp gene from Proteus mirabilis.";
RL J. Mol. Biol. 185:501-507(1985).
CC -!- FUNCTION: A highly abundant outer membrane lipoprotein that controls
CC the distance between the inner and outer membranes. The only protein
CC known to be covalently linked to the peptidoglycan network (PGN). Also
CC non-covalently binds the PGN. The link between the cell outer membrane
CC and PGN contributes to maintenance of the structural and functional
CC integrity of the cell envelope, and maintains the correct distance
CC between the PGN and the outer membrane. {ECO:0000255|HAMAP-
CC Rule:MF_00843}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00843}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00843}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00843};
CC Periplasmic side {ECO:0000255|HAMAP-Rule:MF_00843}. Secreted, cell wall
CC {ECO:0000255|HAMAP-Rule:MF_00843}; Peptidoglycan-anchor
CC {ECO:0000255|HAMAP-Rule:MF_00843}. Note=Attached via its lipidated N-
CC terminus to the inner leaflet of the outer membrane. Attached to the
CC peptidoglycan network (PGN) via its C-terminus. {ECO:0000255|HAMAP-
CC Rule:MF_00843}.
CC -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000255|HAMAP-
CC Rule:MF_00843}.
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DR EMBL; M13176; AAA25658.1; -; Genomic_DNA.
DR EMBL; M28554; AAA25659.1; -; Genomic_DNA.
DR PIR; A24352; A24352.
DR AlphaFoldDB; P09461; -.
DR SMR; P09461; -.
DR STRING; 584.AOUC001_08535; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030258; P:lipid modification; IEA:UniProtKB-UniRule.
DR GO; GO:0043580; P:periplasmic space organization; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00843; Lpp; 1.
DR InterPro; IPR006817; Lipoprotein_leucine-zipper_dom.
DR InterPro; IPR016367; MOM_Lpp.
DR PANTHER; PTHR38763; PTHR38763; 1.
DR Pfam; PF04728; LPP; 1.
DR PIRSF; PIRSF002855; Murein-lipoprotein; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell wall; Coiled coil; Lipoprotein; Membrane;
KW Palmitate; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT CHAIN 20..78
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT /id="PRO_0000018338"
FT REPEAT 25..35
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT REPEAT 39..49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT COILED 28..62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT MOD_RES 78
FT /note="N6-murein peptidoglycan lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
SQ SEQUENCE 78 AA; 8251 MW; 728C5B18E7682B94 CRC64;
MKAKIVLGAV ILASGLLAGC SSSNNAQLDQ ISSDVNRLNT QVQQLSSDVQ SANAQAKAAY
EAARANQRLD NQVTTYKK
