LPP1_SALTY
ID LPP1_SALTY Reviewed; 78 AA.
AC Q7CQN4; Q6VPQ4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Major outer membrane lipoprotein Lpp 1 {ECO:0000255|HAMAP-Rule:MF_00843};
DE AltName: Full=Braun lipoprotein 1 {ECO:0000255|HAMAP-Rule:MF_00843};
DE Short=BLP 1 {ECO:0000255|HAMAP-Rule:MF_00843};
DE AltName: Full=Murein lipoprotein 1 {ECO:0000255|HAMAP-Rule:MF_00843};
DE Flags: Precursor;
GN Name=lpp1 {ECO:0000255|HAMAP-Rule:MF_00843}; Synonyms=lppA;
GN OrderedLocusNames=STM1377;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15213144; DOI=10.1128/iai.72.7.3987-4003.2004;
RA Sha J., Fadl A.A., Klimpel G.R., Niesel D.W., Popov V.L., Chopra A.K.;
RT "The two murein lipoproteins of Salmonella enterica serovar typhimurium
RT contribute to the virulence of the organism.";
RL Infect. Immun. 72:3987-4003(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Plays an important role in virulence (PubMed:15213144). A
CC highly abundant outer membrane lipoprotein that controls the distance
CC between the inner and outer membranes. The only protein known to be
CC covalently linked to the peptidoglycan network (PGN). Also non-
CC covalently binds the PGN. The link between the cell outer membrane and
CC 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 (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_00843, ECO:0000269|PubMed:15213144}.
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 -!- INDUCTION: This gene is probably the major expressed form.
CC {ECO:0000250|UniProtKB:E8XH70}.
CC -!- DISRUPTION PHENOTYPE: The integrity of the cell envelope in a lpp null
CC mutant (double-knockout) is not affected.
CC {ECO:0000269|PubMed:15213144}.
CC -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000255|HAMAP-
CC 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; AY333760; AAR02620.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20301.1; -; Genomic_DNA.
DR RefSeq; NP_460342.1; NC_003197.2.
DR RefSeq; WP_001082307.1; NC_003197.2.
DR AlphaFoldDB; Q7CQN4; -.
DR SMR; Q7CQN4; -.
DR STRING; 99287.STM1377; -.
DR PaxDb; Q7CQN4; -.
DR PRIDE; Q7CQN4; -.
DR EnsemblBacteria; AAL20301; AAL20301; STM1377.
DR GeneID; 1252895; -.
DR GeneID; 67372653; -.
DR KEGG; stm:STM1377; -.
DR PATRIC; fig|99287.12.peg.1460; -.
DR HOGENOM; CLU_166934_2_1_6; -.
DR OMA; QSSAYHK; -.
DR PhylomeDB; Q7CQN4; -.
DR BioCyc; SENT99287:STM1377-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IBA:GO_Central.
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; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT CHAIN 21..78
FT /note="Major outer membrane lipoprotein Lpp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT /id="PRO_0000018344"
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 REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT COMPBIAS 57..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 8391 MW; A362AD45DD5B6A5F CRC64;
MNRTKLVLGA VILGSTLLAG CSSNAKIDQL SSDVQTLNAK VDQLSNDVNA MRSDVQAAKD
DAARANQRLD NQATKYRK
