LPP2_SALT4
ID LPP2_SALT4 Reviewed; 79 AA.
AC E8XH69;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 53.
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}; OrderedLocusNames=STM474_1380;
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74;
RX PubMed=21478351; DOI=10.1128/jb.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
RN [2]
RP NO EXPRESSION.
RC STRAIN=4/74;
RX PubMed=24331466; DOI=10.1016/j.chom.2013.11.010;
RA Kroeger C., Colgan A., Srikumar S., Haendler K., Sivasankaran S.K.,
RA Hammarloef D.L., Canals R., Grissom J.E., Conway T., Hokamp K.,
RA Hinton J.C.;
RT "An infection-relevant transcriptomic compendium for Salmonella enterica
RT Serovar Typhimurium.";
RL Cell Host Microbe 14:683-695(2013).
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: Not expressed under 22 tested conditions.
CC {ECO:0000269|PubMed:24331466}.
CC -!- SIMILARITY: Belongs to the Lpp family. {ECO:0000255|HAMAP-
CC Rule:MF_00843}.
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DR EMBL; CP002487; ADX17076.1; -; Genomic_DNA.
DR RefSeq; WP_001082332.1; NC_016857.1.
DR AlphaFoldDB; E8XH69; -.
DR SMR; E8XH69; -.
DR EnsemblBacteria; ADX17076; ADX17076; STM474_1380.
DR KEGG; seb:STM474_1380; -.
DR PATRIC; fig|909946.3.peg.1417; -.
DR HOGENOM; CLU_166934_2_1_6; -.
DR OMA; ANDRIDN; -.
DR Proteomes; UP000008978; 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_0000447611"
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
