ID   LPP2_SALPA              Reviewed;          79 AA.
AC   Q5PH63;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Major outer membrane lipoprotein Lpp 2 {ECO:0000255|HAMAP-Rule:MF_00843};
DE   AltName: Full=Braun lipoprotein 2 {ECO:0000255|HAMAP-Rule:MF_00843};
DE            Short=BLP 2 {ECO:0000255|HAMAP-Rule:MF_00843};
DE   AltName: Full=Murein lipoprotein 2 {ECO:0000255|HAMAP-Rule:MF_00843};
DE   Flags: Precursor;
GN   Name=lpp2 {ECO:0000255|HAMAP-Rule:MF_00843}; Synonyms=lppB;
GN   OrderedLocusNames=SPA1477;
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 poorly expressed.
CC       {ECO:0000250|UniProtKB:E8XH69}.
CC   -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000255|HAMAP-
CC       Rule:MF_00843}.
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DR   EMBL; CP000026; AAV77414.1; -; Genomic_DNA.
DR   RefSeq; WP_001082322.1; NC_006511.1.
DR   AlphaFoldDB; Q5PH63; -.
DR   SMR; Q5PH63; -.
DR   EnsemblBacteria; AAV77414; AAV77414; SPA1477.
DR   KEGG; spt:SPA1477; -.
DR   HOGENOM; CLU_166934_2_1_6; -.
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   CHAIN           22..79
FT                   /note="Major outer membrane lipoprotein Lpp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT                   /id="PRO_0000018340"
FT   REPEAT          25..35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   REPEAT          39..49
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   REGION          60..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          28..76
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   COMPBIAS        60..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         79
FT                   /note="N6-murein peptidoglycan lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
SQ   SEQUENCE   79 AA;  8441 MW;  9FF884CA9AB0EEE7 CRC64;
     MNRTNKLILG AVVLGSALLA GCSSNAKIDQ LSSDVQTLSA KVDQLSNDVN AMRSDIQAAK
     DDAARANQRL DNKVSRVRK