LPP1_SALPA
ID LPP1_SALPA Reviewed; 78 AA.
AC Q5PH64;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SPA1476;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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:0000255|HAMAP-
CC Rule:MF_00843}.
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 -!- 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; CP000026; AAV77413.1; -; Genomic_DNA.
DR RefSeq; WP_001082307.1; NC_006511.1.
DR AlphaFoldDB; Q5PH64; -.
DR SMR; Q5PH64; -.
DR PRIDE; Q5PH64; -.
DR EnsemblBacteria; AAV77413; AAV77413; SPA1476.
DR GeneID; 67372653; -.
DR KEGG; spt:SPA1476; -.
DR HOGENOM; CLU_166934_2_1_6; -.
DR OMA; QSSAYHK; -.
DR Proteomes; UP000008185; Chromosome.
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 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; Repeat; Secreted; Signal.
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_0000018339"
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
