LPP_SERMA
ID LPP_SERMA Reviewed; 77 AA.
AC P02938;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-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 Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6990409; DOI=10.1073/pnas.77.3.1369;
RA Nakamura K., Inouye M.;
RT "DNA sequence of the Serratia marcescens lipoprotein gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:1369-1373(1980).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V01348; CAA24640.1; -; Genomic_DNA.
DR EMBL; J01789; AAA26566.1; -; Genomic_DNA.
DR PIR; A03438; LPSEW.
DR AlphaFoldDB; P02938; -.
DR SMR; P02938; -.
DR STRING; 273526.SMDB11_1460; -.
DR PRIDE; P02938; -.
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.
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:0000305"
FT CHAIN 20..77
FT /note="Major outer membrane lipoprotein Lpp"
FT /id="PRO_0000018346"
FT REPEAT 23..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT REPEAT 37..47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT REGION 56..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT MOD_RES 77
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 77 AA; 8239 MW; D496026FED17E6AA CRC64;
MNRTKLVLGA VILGSHSAGC SSNAKIDQLS SDVQTLNAKV DQLSNDVNAM RSDVQAAKDD
AARANQRLDN QAHAYKK