ID Q6LJB4_PHOPR Unreviewed; 87 AA.
AC Q6LJB4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Major outer membrane lipoprotein Lpp {ECO:0000256|HAMAP-Rule:MF_00843};
GN Name=STM1377 {ECO:0000313|EMBL:CAG22616.1};
GN Synonyms=lpp {ECO:0000256|HAMAP-Rule:MF_00843};
GN OrderedLocusNames=PBPRB0744 {ECO:0000313|EMBL:CAG22616.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22616.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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}.
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DR EMBL; CR378677; CAG22616.1; -; Genomic_DNA.
DR RefSeq; WP_006229590.1; NC_006371.1.
DR AlphaFoldDB; Q6LJB4; -.
DR STRING; 298386.PBPRB0744; -.
DR KEGG; ppr:PBPRB0744; -.
DR eggNOG; COG4238; Bacteria.
DR HOGENOM; CLU_166934_1_0_6; -.
DR Proteomes; UP000000593; Chromosome 2.
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:UP000000593};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..87
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004276750"
FT REPEAT 33..43
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843"
FT DOMAIN 35..87
FT /note="Lipoprotein leucine-zipper"
FT /evidence="ECO:0000259|Pfam:PF04728"
FT MOD_RES 87
FT /note="N6-murein peptidoglycan lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-1"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
SQ SEQUENCE 87 AA; 9316 MW; F64387EDA4E51026 CRC64;
MNRSLTILSG VILSAALMGC SSSDEVDQMQ QLTNKVDMLS DQVSALQSQQ DQMAGAVNDS
RAASDAAYQE AMRANQRIDN IAGSYTK
//
