ID A0A1R4B665_9VIBR Unreviewed; 89 AA.
AC A0A1R4B665;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Major outer membrane lipoprotein Lpp {ECO:0000256|HAMAP-Rule:MF_00843};
GN Name=lpp {ECO:0000256|HAMAP-Rule:MF_00843,
GN ECO:0000313|EMBL:SJL84409.1};
GN ORFNames=VPAL9027_02393 {ECO:0000313|EMBL:SJL84409.1};
OS Vibrio palustris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1918946 {ECO:0000313|EMBL:SJL84409.1, ECO:0000313|Proteomes:UP000189475};
RN [1] {ECO:0000313|EMBL:SJL84409.1, ECO:0000313|Proteomes:UP000189475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 9027 {ECO:0000313|EMBL:SJL84409.1,
RC ECO:0000313|Proteomes:UP000189475};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; FUFT01000005; SJL84409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4B665; -.
DR STRING; 1918946.VPAL9027_02393; -.
DR OrthoDB; 5593828at2; -.
DR Proteomes; UP000189475; 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:UP000189475};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..89
FT /note="Major outer membrane lipoprotein Lpp"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013159209"
FT REPEAT 35..45
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843"
FT DOMAIN 37..89
FT /note="Lipoprotein leucine-zipper"
FT /evidence="ECO:0000259|Pfam:PF04728"
FT REGION 52..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="N6-murein peptidoglycan lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-1"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00843,
FT ECO:0000256|PIRSR:PIRSR002855-2"
SQ SEQUENCE 89 AA; 9354 MW; E99F96F0D971A429 CRC64;
MNKMLLAAAT SSVLLLAGCA SGTNEATTSK LDNLTDQVEQ LQDEVASLKS EHAALASKTN
QSADAAMAAQ DEAQRANKRI DNIAQSYTK
//
