LPP_ECOLI
ID LPP_ECOLI Reviewed; 78 AA.
AC P69776; P02937; Q53272;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Major outer membrane lipoprotein Lpp {ECO:0000255|HAMAP-Rule:MF_00843};
DE AltName: Full=Braun lipoprotein {ECO:0000255|HAMAP-Rule:MF_00843};
DE Short=BLP {ECO:0000255|HAMAP-Rule:MF_00843};
DE AltName: Full=Murein-lipoprotein {ECO:0000255|HAMAP-Rule:MF_00843, ECO:0000303|PubMed:4261992};
DE Flags: Precursor;
GN Name=lpp {ECO:0000255|HAMAP-Rule:MF_00843}; Synonyms=mlpA, mulI;
GN OrderedLocusNames=b1677, JW1667;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=391404; DOI=10.1016/0092-8674(79)90224-1;
RA Nakamura K., Inouye M.;
RT "DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an
RT extremely AT-rich promoter.";
RL Cell 18:1109-1117(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6765942; DOI=10.1016/s0021-9258(19)86285-3;
RA Nakamura K., Pirtle R.M., Pirtle I.L., Takeishi K., Inouye M.;
RT "Messenger ribonucleic acid of the lipoprotein of the Escherichia coli
RT outer membrane. II. The complete nucleotide sequence.";
RL J. Biol. Chem. 255:210-216(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-20 (PRECURSOR PROTEIN), AND FORMYLATION AT MET-1.
RX PubMed=322142; DOI=10.1073/pnas.74.3.1004;
RA Inouye S., Wang S., Sekizawa J., Halegoua S., Inouye M.;
RT "Amino acid sequence for the peptide extension on the prolipoprotein of the
RT Escherichia coli outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:1004-1008(1977).
RN [7]
RP PROTEIN SEQUENCE OF 21-78, FUNCTION, SUBCELLULAR LOCATION, AND C-TERMINAL
RP ATTACHMENT TO PEPTIDOGLYCAN.
RC STRAIN=B;
RX PubMed=4261992; DOI=10.1111/j.1432-1033.1972.tb01883.x;
RA Braun V., Bosch V.;
RT "Sequence of the murein-lipoprotein and the attachment site of the lipid.";
RL Eur. J. Biochem. 28:51-69(1972).
RN [8]
RP PROTEIN SEQUENCE OF 21-24, DIACYLGLYCEROL AT CYS-21, PALMITOYLATION AT
RP CYS-21, AND SUBCELLULAR LOCATION.
RC STRAIN=B/r;
RX PubMed=4575979; DOI=10.1111/j.1432-1033.1973.tb02757.x;
RA Hantke K., Braun V.;
RT "Covalent binding of lipid to protein. Diglyceride and amide-linked fatty
RT acid at the N-terminal end of the murein-lipoprotein of the Escherichia
RT coli outer membrane.";
RL Eur. J. Biochem. 34:284-296(1973).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-78.
RC STRAIN=SK5726;
RX PubMed=1380161; DOI=10.1073/pnas.89.16.7546;
RA Cao G.J., Sarkar N.;
RT "Poly(A) RNA in Escherichia coli: nucleotide sequence at the junction of
RT the lpp transcript and the polyadenylate moiety.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7546-7550(1992).
RN [10]
RP PROTEIN SEQUENCE OF 77-78, FUNCTION, SUBCELLULAR LOCATION, LIPID-ANCHOR,
RP AND C-TERMINAL ATTACHMENT TO PEPTIDOGLYCAN.
RC STRAIN=B/r, and K12 / W945;
RX PubMed=4245367; DOI=10.1111/j.1432-1033.1970.tb00936.x;
RA Braun V., Sieglin U.;
RT "The covalent murein-lipoprotein structure of the Escherichia coli cell
RT wall. The attachment site of the lipoprotein on the murein.";
RL Eur. J. Biochem. 13:336-346(1970).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND PEPTIDOGLYCAN-BOUND AND NON-BOUND
RP FORMS.
RC STRAIN=K12 / KL16, and K12 / MX74T2;
RX PubMed=4565677; DOI=10.1016/s0021-9258(20)81822-5;
RA Inouye M., Shaw J., Shen C.;
RT "The assembly of a structural lipoprotein in the envelope of Escherichia
RT coli.";
RL J. Biol. Chem. 247:8154-8159(1972).
RN [12]
RP MUTANTS ALTER OUTER MEMBRANE SHAPE AND INTEGRITY, AND DISRUPTION PHENOTYPE.
RX PubMed=361695; DOI=10.1128/jb.136.1.280-285.1978;
RA Sonntag I., Schwarz H., Hirota Y., Henning U.;
RT "Cell envelope and shape of Escherichia coli: multiple mutants missing the
RT outer membrane lipoprotein and other major outer membrane proteins.";
RL J. Bacteriol. 136:280-285(1978).
RN [13] {ECO:0000305}
RP SUBUNIT, INTERACTION WITH OMPA, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / SM1006;
RX PubMed=3013869; DOI=10.1016/s0021-9258(19)84474-5;
RA Choi D.-S., Yamada H., Mizuno T., Mizushima S.;
RT "Trimeric structure and localization of the major lipoprotein in the cell
RT surface of Escherichia coli.";
RL J. Biol. Chem. 261:8953-8957(1986).
RN [14]
RP MUTAGENESIS OF ASP-70; LYS-75; TYR-76; ARG-77 AND LYS-78.
RC STRAIN=K12;
RX PubMed=1527073; DOI=10.1016/s0021-9258(18)41811-x;
RA Zhang W.-Y., Wu H.C.;
RT "Alterations of the carboxyl-terminal amino acid residues of Escherichia
RT coli lipoprotein affect the formation of murein-bound lipoprotein.";
RL J. Biol. Chem. 267:19560-19564(1992).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP MUTAGENESIS OF SER-22.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=9139900; DOI=10.1128/jb.179.9.2857-2862.1997;
RA Yakushi T., Tajima T., Matsuyama S., Tokuda H.;
RT "Lethality of the covalent linkage between mislocalized major outer
RT membrane lipoprotein and the peptidoglycan of Escherichia coli.";
RL J. Bacteriol. 179:2857-2862(1997).
RN [17]
RP INTERACTION WITH TOLB.
RX PubMed=9701827; DOI=10.1046/j.1365-2958.1998.00945.x;
RA Clavel T., Germon P., Vianney A., Portalier R., Lazzaroni J.-C.;
RT "TolB protein of Escherichia coli K-12 interacts with the outer membrane
RT peptidoglycan-associated proteins Pal, Lpp and OmpA.";
RL Mol. Microbiol. 29:359-367(1998).
RN [18]
RP INTERACTION WITH PAL.
RX PubMed=11790745; DOI=10.1128/jb.184.3.754-759.2002;
RA Cascales E., Bernadac A., Gavioli M., Lazzaroni J.-C., Lloubes R.;
RT "Pal lipoprotein of Escherichia coli plays a major role in outer membrane
RT integrity.";
RL J. Bacteriol. 184:754-759(2002).
RN [19]
RP INTERACTION WITH TONB.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11872715; DOI=10.1128/jb.184.6.1640-1648.2002;
RA Higgs P.I., Letain T.E., Merriam K.K., Burke N.S., Park H., Kang C.,
RA Postle K.;
RT "TonB interacts with nonreceptor proteins in the outer membrane of
RT Escherichia coli.";
RL J. Bacteriol. 184:1640-1648(2002).
RN [20]
RP TRANSLOCATION BY SRP/SEC/YIDC PATHWAY.
RX PubMed=15140892; DOI=10.1074/jbc.m403229200;
RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.;
RT "Targeting and translocation of two lipoproteins in Escherichia coli via
RT the SRP/Sec/YidC pathway.";
RL J. Biol. Chem. 279:31026-31032(2004).
RN [21] {ECO:0000305}
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [22]
RP SUBCELLULAR LOCATION OF NON-PEPTIDOGLYCAN-BOUND FORM, AND MUTAGENESIS OF
RP 37-LEU--ALA-57; 75-LYS--LYS-78 AND LYS-78.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=21219470; DOI=10.1111/j.1365-2958.2011.07539.x;
RA Cowles C.E., Li Y., Semmelhack M.F., Cristea I.M., Silhavy T.J.;
RT "The free and bound forms of Lpp occupy distinct subcellular locations in
RT Escherichia coli.";
RL Mol. Microbiol. 79:1168-1181(2011).
RN [23]
RP PROTEIN COPY NUMBER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24766808; DOI=10.1016/j.cell.2014.02.033;
RA Li G.W., Burkhardt D., Gross C., Weissman J.S.;
RT "Quantifying absolute protein synthesis rates reveals principles underlying
RT allocation of cellular resources.";
RL Cell 157:624-635(2014).
RN [24]
RP CONTROLS PERIPLASMIC WIDTH, AND MUTAGENESIS OF GLN-43 AND LYS-78.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=29257832; DOI=10.1371/journal.pbio.2004303;
RA Asmar A.T., Ferreira J.L., Cohen E.J., Cho S.H., Beeby M., Hughes K.T.,
RA Collet J.F.;
RT "Communication across the bacterial cell envelope depends on the size of
RT the periplasm.";
RL PLoS Biol. 15:E2004303-E2004303(2017).
RN [25]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=28978443; DOI=10.1016/j.bpj.2017.08.011;
RA Samsudin F., Boags A., Piggot T.J., Khalid S.;
RT "Braun's lipoprotein facilitates OmpA interaction with the Escherichia coli
RT cell wall.";
RL Biophys. J. 113:1496-1504(2017).
RN [26]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=30713026; DOI=10.1016/j.str.2019.01.001;
RA Boags A.T., Samsudin F., Khalid S.;
RT "Binding from both sides: TolR and full-length OmpA bind and maintain the
RT local structure of the E. coli cell wall.";
RL Structure 27:713-724(2019).
RN [27]
RP 3D-STRUCTURE MODELING.
RX PubMed=353292; DOI=10.1016/0022-2836(78)90396-0;
RA McLachlan A.D.;
RT "The double helix coiled coil structure of murein lipoprotein from
RT Escherichia coli.";
RL J. Mol. Biol. 121:493-506(1978).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 22-77, AND SUBUNIT.
RX PubMed=10843861; DOI=10.1006/jmbi.2000.3776;
RA Shu W., Liu J., Ji H., Lu M.;
RT "Core structure of the outer membrane lipoprotein from Escherichia coli at
RT 1.9 A resolution.";
RL J. Mol. Biol. 299:1101-1112(2000).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 22-71 OF MUTANT ALA-14.
RX PubMed=12368282; DOI=10.1074/jbc.m208773200;
RA Liu J., Lu M.;
RT "An alanine-zipper structure determined by long range intermolecular
RT interactions.";
RL J. Biol. Chem. 277:48708-48713(2002).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-77 OF MUTANTS ALA-5 AND ALA-7.
RX PubMed=12054830; DOI=10.1016/s0022-2836(02)00138-9;
RA Liu J., Cao W., Lu M.;
RT "Core side-chain packing and backbone conformation in Lpp-56 coiled-coil
RT mutants.";
RL J. Mol. Biol. 318:877-888(2002).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-77 OF MUTANT ALA-10(56).
RX PubMed=12741822; DOI=10.1021/bi026828a;
RA Liu J., Dai J., Lu M.;
RT "Zinc-mediated helix capping in a triple-helical protein.";
RL Biochemistry 42:5657-5664(2003).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 22-73 OF MUTANT TRP-14.
RX PubMed=15520380; DOI=10.1073/pnas.0405319101;
RA Liu J., Yong W., Deng Y., Kallenbach N.R., Lu M.;
RT "Atomic structure of a tryptophan-zipper pentamer.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16156-16161(2004).
CC -!- FUNCTION: An outer membrane lipoprotein that controls the distance
CC between the inner and outer membranes; adding residues to Lpp increases
CC the width of the periplasm (PubMed:29257832). The only protein known to
CC be covalently linked to the peptidoglycan network (PGN)
CC (PubMed:4261992, PubMed:3013869, PubMed:4245367). Also non-covalently
CC binds the PGN (PubMed:3013869). The link between the cell outer
CC membrane and PGN contributes to the maintenance of the structural and
CC functional integrity of the cell envelope, and maintains the correct
CC distance between the PGN and the outer membrane (PubMed:4261992,
CC PubMed:3013869, PubMed:4245367, PubMed:4565677). The most abundant
CC cellular protein in terms of copy number, there can be up to one
CC million Lpp molecules per cell (PubMed:24766808). About one-third of
CC Lpp is bound to the PGN (called bound or periplasmic) the rest is
CC called free or transmembrane (PubMed:4565677). The 'free' form can be
CC surface labeled by membrane impermeable agents and so must cross the
CC outer membrane; it is thought that this transmembrane form is still
CC anchored in the inner leaflet of the outer membrane (PubMed:21219470).
CC Modeling suggests that non-covalent binding of OmpA (from the outer
CC membrane) and TolR (from the inner membrane) to peptidoglycan maintains
CC the position of the cell wall in the periplasm, holding it
CC approximately equidistant from both the inner and outer membranes.
CC Trimeric Lpp controls the width of the periplasm, adjusts its tilt
CC angle to accommodate to the available space, and can compensate in part
CC for an absence of OmpA (Probable). The role of the cell surface-
CC exposed, free form (transmembrane) of Lpp is unknown (PubMed:21219470).
CC {ECO:0000269|PubMed:21219470, ECO:0000269|PubMed:24766808,
CC ECO:0000269|PubMed:29257832, ECO:0000269|PubMed:3013869,
CC ECO:0000269|PubMed:4245367, ECO:0000269|PubMed:4261992,
CC ECO:0000269|PubMed:4565677, ECO:0000305|PubMed:28978443,
CC ECO:0000305|PubMed:30713026}.
CC -!- SUBUNIT: Homotrimer (PubMed:3013869, PubMed:10843861). Interacts with
CC OmpA (PubMed:3013869). Has been isolated from outer membrane
CC preparations as an approximately 87 kDa complex, suggesting it also
CC forms larger complexes (PubMed:16079137). Seems to interact with TolB,
CC Pal and TonB (PubMed:9701827). {ECO:0000269|PubMed:10843861,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:3013869,
CC ECO:0000269|PubMed:9701827}.
CC -!- INTERACTION:
CC P69776; P69776: lpp; NbExp=2; IntAct=EBI-909750, EBI-909750;
CC P69776; P02929: tonB; NbExp=2; IntAct=EBI-909750, EBI-6399993;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00843, ECO:0000269|PubMed:3013869, ECO:0000305|PubMed:4245367};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00843,
CC ECO:0000269|PubMed:3013869, ECO:0000269|PubMed:4245367,
CC ECO:0000269|PubMed:4575979}; Periplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_00843, ECO:0000269|PubMed:4575979}. Secreted, cell wall
CC {ECO:0000255|HAMAP-Rule:MF_00843, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:4245367, ECO:0000269|PubMed:4565677}; Peptidoglycan-
CC anchor {ECO:0000255|HAMAP-Rule:MF_00843, ECO:0000269|PubMed:4245367,
CC ECO:0000269|PubMed:4261992, ECO:0000269|PubMed:4565677,
CC ECO:0000305|PubMed:16079137}. Cell outer membrane
CC {ECO:0000269|PubMed:21219470}; Lipid-anchor
CC {ECO:0000305|PubMed:21219470}; Extracellular side
CC {ECO:0000269|PubMed:21219470}. Note=Attached via its lipidated N-
CC terminus to the inner leaflet of the outer membrane (PubMed:4575979).
CC Attached to the peptidoglycan network (PGN) via its C-terminus
CC (PubMed:4261992, PubMed:4245367) (Probable). About one-third of the
CC protein links the outer membrane and the PGN, the rest is not-linked to
CC PGN. PGN-bound and non-bound forms can interconvert (PubMed:4565677).
CC The C-terminus of the non-PGN-bound form is exposed on the cell
CC surface; its N-terminus is probably anchored in the inner leaflet
CC (PubMed:21219470). Targeted by the SRP/Sec/YidC pathway
CC (PubMed:15140892). {ECO:0000269|PubMed:15140892,
CC ECO:0000269|PubMed:21219470, ECO:0000269|PubMed:4245367,
CC ECO:0000269|PubMed:4261992, ECO:0000269|PubMed:4565677,
CC ECO:0000269|PubMed:4575979, ECO:0000305|PubMed:3013869,
CC ECO:0000305|PubMed:4565677}.
CC -!- DISRUPTION PHENOTYPE: Double lpp-ompA mutants are spherical and only
CC grow in the presence of electrolytes such as 30 mM Mg(2+), and are
CC sensitive to hydrophobic antibiotics and detergents. The peptidoglycan
CC layer is no longer attached to the cell outer membrane which undergoes
CC abundant blebbing. {ECO:0000269|PubMed:361695}.
CC -!- MISCELLANEOUS: About one-third of Lpp is covalently bound to
CC peptidoglycan. {ECO:0000269|PubMed:4565677}.
CC -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000255|HAMAP-
CC Rule:MF_00843}.
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DR EMBL; V00302; CAA23580.1; -; Genomic_DNA.
DR EMBL; X68953; CAA48767.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74747.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16044.1; -; Genomic_DNA.
DR EMBL; S42225; AAB22836.1; -; mRNA.
DR PIR; A90783; LPECW.
DR RefSeq; NP_416192.1; NC_000913.3.
DR RefSeq; WP_000648420.1; NZ_STEB01000003.1.
DR PDB; 1EQ7; X-ray; 1.90 A; A=22-77.
DR PDB; 1JCC; X-ray; 1.70 A; A/B/C=22-77.
DR PDB; 1JCD; X-ray; 1.30 A; A/B/C=22-73.
DR PDB; 1KFM; X-ray; 2.00 A; A=22-77.
DR PDB; 1KFN; X-ray; 1.65 A; A=22-77.
DR PDB; 1T8Z; X-ray; 1.45 A; A/B/C/D/E=22-74.
DR PDB; 2GUS; X-ray; 1.75 A; A=22-77.
DR PDB; 2GUV; X-ray; 1.40 A; A/B/C/D/E=22-77.
DR PDB; 7ARH; EM; 3.30 A; V=21-30.
DR PDB; 7ARJ; EM; 3.20 A; V=21-30.
DR PDB; 7ARL; EM; 3.20 A; V=21-30.
DR PDB; 7ARM; EM; 3.60 A; V=21-30.
DR PDBsum; 1EQ7; -.
DR PDBsum; 1JCC; -.
DR PDBsum; 1JCD; -.
DR PDBsum; 1KFM; -.
DR PDBsum; 1KFN; -.
DR PDBsum; 1T8Z; -.
DR PDBsum; 2GUS; -.
DR PDBsum; 2GUV; -.
DR PDBsum; 7ARH; -.
DR PDBsum; 7ARJ; -.
DR PDBsum; 7ARL; -.
DR PDBsum; 7ARM; -.
DR AlphaFoldDB; P69776; -.
DR SMR; P69776; -.
DR BioGRID; 4260276; 199.
DR DIP; DIP-35674N; -.
DR IntAct; P69776; 6.
DR STRING; 511145.b1677; -.
DR TCDB; 8.A.99.1.1; the blp braun's lipoprotein (lpp) family.
DR jPOST; P69776; -.
DR PaxDb; P69776; -.
DR PRIDE; P69776; -.
DR EnsemblBacteria; AAC74747; AAC74747; b1677.
DR EnsemblBacteria; BAA16044; BAA16044; BAA16044.
DR GeneID; 67415618; -.
DR GeneID; 946175; -.
DR KEGG; ecj:JW1667; -.
DR KEGG; eco:b1677; -.
DR PATRIC; fig|1411691.4.peg.581; -.
DR EchoBASE; EB0539; -.
DR eggNOG; COG4238; Bacteria.
DR HOGENOM; CLU_166934_2_1_6; -.
DR OMA; ANDRIDN; -.
DR PhylomeDB; P69776; -.
DR BioCyc; EcoCyc:EG10544-MON; -.
DR EvolutionaryTrace; P69776; -.
DR PRO; PR:P69776; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; NAS:UniProtKB.
DR GO; GO:0042834; F:peptidoglycan binding; TAS:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IMP:UniProtKB.
DR GO; GO:0043580; P:periplasmic space organization; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall; Coiled coil;
KW Direct protein sequencing; Formylation; Lipoprotein; Membrane; Palmitate;
KW Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843,
FT ECO:0000269|PubMed:4261992, ECO:0000269|PubMed:4575979"
FT CHAIN 21..78
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT /id="PRO_0000018331"
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 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:322142"
FT MOD_RES 78
FT /note="N6-murein peptidoglycan lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843,
FT ECO:0000269|PubMed:4245367, ECO:0000269|PubMed:4261992"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843,
FT ECO:0000269|PubMed:4575979"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843,
FT ECO:0000269|PubMed:4575979"
FT VARIANT 29
FT /note="Q -> E (in strain: B)"
FT /evidence="ECO:0000269|PubMed:4261992"
FT MUTAGEN 22
FT /note="S->D: Localizes to the inner membrane, where it
FT associates with peptidoglycan, thereby preventing
FT separation of the two membranes. Prolonged expression is
FT lethal for the cell."
FT /evidence="ECO:0000269|PubMed:9139900"
FT MUTAGEN 37..57
FT /note="Missing: Does not affect the formation of murein-
FT bound lipoprotein, has almost no surface-exposed Lpp. Cells
FT are mucoid."
FT /evidence="ECO:0000269|PubMed:21219470"
FT MUTAGEN 43
FT /note="Q->TLSAKVEQLSNDVNAMRSDVDQ: Periplasm is 4 nm larger
FT than wild-type, cells no longer trigger Rcs system."
FT /evidence="ECO:0000269|PubMed:29257832"
FT MUTAGEN 43
FT /note="Q->TLSAKVEQLSNDVNQ: Periplasm is 3 nm larger than
FT wild-type, cells no longer trigger Rcs system."
FT /evidence="ECO:0000269|PubMed:29257832"
FT MUTAGEN 70
FT /note="D->E,G,S: Does not affect the formation of murein-
FT bound lipoprotein."
FT /evidence="ECO:0000269|PubMed:1527073"
FT MUTAGEN 75..78
FT /note="Missing: Protein is no longer biotinylated on the
FT cell surface."
FT /evidence="ECO:0000269|PubMed:21219470"
FT MUTAGEN 75
FT /note="K->S,T: Does not affect the formation of murein-
FT bound lipoprotein."
FT /evidence="ECO:0000269|PubMed:1527073"
FT MUTAGEN 76
FT /note="Y->C,D,E,G,N,P,S: Reduces the formation of murein-
FT bound lipoprotein."
FT /evidence="ECO:0000269|PubMed:1527073"
FT MUTAGEN 76
FT /note="Y->F,H,I,L: Does not affect the formation of murein-
FT bound lipoprotein."
FT /evidence="ECO:0000269|PubMed:1527073"
FT MUTAGEN 77
FT /note="R->D,L: Reduces the formation of murein-bound
FT lipoprotein."
FT /evidence="ECO:0000269|PubMed:1527073"
FT MUTAGEN 78
FT /note="K->R: Abolishes the formation of murein-bound
FT lipoprotein. Reduced biotinylation on the cell surface."
FT /evidence="ECO:0000269|PubMed:1527073,
FT ECO:0000269|PubMed:21219470"
FT MUTAGEN 78
FT /note="Missing: Cells no longer trigger Rcs system, outer
FT membrane forms blebs, periplasm is about 3 nm larger than
FT wild-type."
FT /evidence="ECO:0000269|PubMed:29257832"
FT HELIX 25..71
FT /evidence="ECO:0007829|PDB:1JCD"
SQ SEQUENCE 78 AA; 8323 MW; 19F41D5251913C93 CRC64;
MKATKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA MRSDVQAAKD
DAARANQRLD NMATKYRK
