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LPP2_SALTY
ID   LPP2_SALTY              Reviewed;          79 AA.
AC   Q8ZPP9; Q6VPQ3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=STM1376;
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 poorly expressed.
CC       {ECO:0000250|UniProtKB:E8XH69}.
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}.
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DR   EMBL; AY333760; AAR02621.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20300.1; -; Genomic_DNA.
DR   RefSeq; NP_460341.1; NC_003197.2.
DR   RefSeq; WP_001082332.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPP9; -.
DR   SMR; Q8ZPP9; -.
DR   STRING; 99287.STM1376; -.
DR   PaxDb; Q8ZPP9; -.
DR   EnsemblBacteria; AAL20300; AAL20300; STM1376.
DR   GeneID; 1252894; -.
DR   KEGG; stm:STM1376; -.
DR   PATRIC; fig|99287.12.peg.1459; -.
DR   HOGENOM; CLU_166934_2_1_6; -.
DR   OMA; ANDRIDN; -.
DR   PhylomeDB; Q8ZPP9; -.
DR   BioCyc; SENT99287:STM1376-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..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_0000018345"
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   COILED          28..69
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00843"
FT   MOD_RES         79
FT                   /note="N6-murein peptidoglycan lysine"
FT                   /evidence="ECO:0000305"
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;  8492 MW;  CE0DA4D89B851354 CRC64;
     MNRTNQLILG AVVLGSTLLA GCSSNAKIDQ LSSDVQTLSA KVEQLSNDVN AMRSDVQAAK
     DDAARANQRL DNKVFRICK
 
 
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