PAL_LEGPN
ID PAL_LEGPN Reviewed; 176 AA.
AC P26493;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000255|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000255|HAMAP-Rule:MF_02204};
DE AltName: Full=19 kDa surface antigen;
DE AltName: Full=PPL;
DE Flags: Precursor;
GN Name=pal {ECO:0000255|HAMAP-Rule:MF_02204}; Synonyms=pplA;
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AA100 / Serogroup 1;
RX PubMed=1766377; DOI=10.1111/j.1365-2958.1991.tb00824.x;
RA Engleberg N.C., Howe D.C., Rogers J.E., Arroyo J., Eisenstein B.I.;
RT "Characterization of a Legionella pneumophila gene encoding a lipoprotein
RT antigen.";
RL Mol. Microbiol. 5:2021-2029(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1855972; DOI=10.1128/iai.59.8.2515-2521.1991;
RA Ludwig B., Schmid A., Marre R., Hacker J.;
RT "Cloning, genetic analysis, and nucleotide sequence of a determinant coding
RT for a 19-kilodalton peptidoglycan-associated protein (Ppl) of Legionella
RT pneumophila.";
RL Infect. Immun. 59:2515-2521(1991).
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity (By similarity). Very strongly
CC associated with the peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer.
CC {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02204}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; X60543; CAA43033.1; -; Genomic_DNA.
DR PIR; A60337; A60337.
DR RefSeq; WP_010947759.1; NZ_UGOV01000002.1.
DR AlphaFoldDB; P26493; -.
DR SMR; P26493; -.
DR STRING; 91892.BIZ52_10025; -.
DR GeneID; 66491175; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; ESNESCW; -.
DR OrthoDB; 1544679at2; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_02204; Pal; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR039001; Pal.
DR InterPro; IPR014169; Pal_lipo_C.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR TIGRFAMs; TIGR02802; Pal_lipo; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell outer membrane; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT CHAIN 22..176
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT /id="PRO_0000020124"
FT DOMAIN 60..176
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
SQ SEQUENCE 176 AA; 18911 MW; 7D9C3EBECBE621DB CRC64;
MKAGSFYKLG LLVASAVLVA ACSKTPGSAD GGAAVGDGDA TAQGLGQMTH FAGQEPGESY
TTQAPHNQLY LFAYDDSTLA SKYLPSVNAQ AEYLKTHPGA RVMIAGHTDE RGSREYNVAL
GERRADTVAE ILRMAGVSRQ QIRVVSYGKE RPANYGHDEA SHAQNRRVEF IYEATR