ID   LPP_PECAS               Reviewed;          78 AA.
AC   Q6D622;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, 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}; OrderedLocusNames=ECA1866;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG74769.1; -; Genomic_DNA.
DR   RefSeq; WP_005970385.1; NC_004547.2.
DR   AlphaFoldDB; Q6D622; -.
DR   SMR; Q6D622; -.
DR   STRING; 218491.ECA1866; -.
DR   PRIDE; Q6D622; -.
DR   EnsemblBacteria; CAG74769; CAG74769; ECA1866.
DR   GeneID; 51389298; -.
DR   GeneID; 61408465; -.
DR   GeneID; 66803108; -.
DR   KEGG; eca:ECA1866; -.
DR   eggNOG; COG4238; Bacteria.
DR   HOGENOM; CLU_166934_2_1_6; -.
DR   OMA; QSSAYHK; -.
DR   OrthoDB; 1991143at2; -.
DR   Proteomes; UP000007966; Chromosome.
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; Reference proteome; Repeat; Secreted;
KW   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_0000018335"
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          27..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;  8401 MW;  A3759D5308A07A5F CRC64;
     MNRTKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA IRSDVQAAKD
     DAARANQRLD NQVRTYKK