LPP_ERWAM
ID LPP_ERWAM Reviewed; 78 AA.
AC P02939;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Erwinia amylovora (Fire blight bacteria).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=552;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6257705; DOI=10.1016/s0021-9258(19)69759-0;
RA Yamagata H., Nakamura K., Inouye M.;
RT "Comparison of the lipoprotein gene among the Enterobacteriaceae. DNA
RT sequence of Erwinia amylovora lipoprotein gene.";
RL J. Biol. Chem. 256:2194-2198(1981).
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; J01577; AAA24824.1; -; Genomic_DNA.
DR PIR; A03439; NPWCWY.
DR RefSeq; WP_004157411.1; NZ_RQKG01000001.1.
DR AlphaFoldDB; P02939; -.
DR SMR; P02939; -.
DR GeneID; 8914042; -.
DR OMA; QSSAYHK; -.
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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT CHAIN 21..78
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT /id="PRO_0000018334"
FT REPEAT 24..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT REPEAT 38..48
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT COILED 22..75
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 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
SQ SEQUENCE 78 AA; 8369 MW; 0367FD570D44CD53 CRC64;
MNRTKLVLGA VILGSTLLAG CSSNAKIDQL STDVQTLNAK VDQLSNDVTA IRSDVQAAKD
DAARANQRLD NQAHSYRK
