ID A0A0L7T6E6_9GAMM Unreviewed; 78 AA.
AC A0A0L7T6E6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Major outer membrane lipoprotein Lpp {ECO:0000256|HAMAP-Rule:MF_00843};
GN Name=lpp {ECO:0000256|HAMAP-Rule:MF_00843};
GN ORFNames=NG42_07640 {ECO:0000313|EMBL:KOC90913.1}, NG43_07225
GN {ECO:0000313|EMBL:KOC93995.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC90913.1, ECO:0000313|Proteomes:UP000037088};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC90913.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC93995.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:0000256|HAMAP-
CC Rule:MF_00843}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00843}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_00843}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00843};
CC Periplasmic side {ECO:0000256|HAMAP-Rule:MF_00843}. Secreted, cell wall
CC {ECO:0000256|HAMAP-Rule:MF_00843}; Peptidoglycan-anchor
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00843}.
CC -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000256|HAMAP-
CC Rule:MF_00843}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00843}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOC90913.1}.
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DR EMBL; JRXE01000008; KOC90913.1; -; Genomic_DNA.
DR EMBL; JRXF01000009; KOC93995.1; -; Genomic_DNA.
DR RefSeq; WP_052898670.1; NZ_JRXF01000009.1.
DR AlphaFoldDB; A0A0L7T6E6; -.
DR STRING; 1560201.NG42_07640; -.
DR GeneID; 84613284; -.
DR PATRIC; fig|1560201.3.peg.1628; -.
DR OrthoDB; 6567756at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
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 Gene3D; 1.20.5.190; -; 1.
DR HAMAP; MF_00843; Lpp; 1.
DR InterPro; IPR006817; Lipoprotein_leucine-zipper_dom.
DR InterPro; IPR016367; MOM_Lpp.
DR NCBIfam; NF040598; Ala_zip_lipo; 1.
DR PANTHER; PTHR38763:SF1; MAJOR OUTER MEMBRANE LIPOPROTEIN LPP; 1.
DR PANTHER; PTHR38763; MAJOR OUTER MEMBRANE PROLIPOPROTEIN LPP; 1.
DR Pfam; PF04728; LPP; 1.
DR PIRSF; PIRSF002855; Murein-lipoprotein; 1.
DR SUPFAM; SSF58042; Outer membrane lipoprotein; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_00843}; Cell wall {ECO:0000256|HAMAP-Rule:MF_00843};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_00843};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00843};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_00843};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088, ECO:0000256|HAMAP-
KW Rule:MF_00843}; Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00843};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_00843};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..78
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010427043"
FT DOMAIN 26..78
FT /note="Lipoprotein leucine-zipper"
FT /evidence="ECO:0000259|Pfam:PF04728"
FT REPEAT 38..48
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="N6-murein peptidoglycan lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-1"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
SQ SEQUENCE 78 AA; 8368 MW; 0367FD49FCB06CE9 CRC64;
MNRTKLVLGA VILGSTLLAG CSSNAKIDQL STDVQTLNAK VDQLSNDVNA VRSDVQAAKD
DAARANQRLD NQAHSYRK
//
