PAL_PSEPU
ID PAL_PSEPU Reviewed; 166 AA.
AC P0A139; P43036;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000255|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000255|HAMAP-Rule:MF_02204};
DE Flags: Precursor;
GN Name=pal {ECO:0000255|HAMAP-Rule:MF_02204}; Synonyms=oprL, pal1;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX PubMed=8626299; DOI=10.1128/jb.178.6.1699-1706.1996;
RA Rodriguez-Herva J.J., Ramos-Gonzalez M.I., Ramos J.L.;
RT "The Pseudomonas putida peptidoglycan-associated outer membrane lipoprotein
RT is involved in maintenance of the integrity of the cell cell envelope.";
RL J. Bacteriol. 178:1699-1706(1996).
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. {ECO:0000255|HAMAP-
CC 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; X74218; CAA52294.1; -; Genomic_DNA.
DR PIR; S52308; S52308.
DR RefSeq; WP_003254755.1; NZ_VCPS01000019.1.
DR AlphaFoldDB; P0A139; -.
DR SMR; P0A139; -.
DR STRING; 1240350.AMZE01000017_gene3890; -.
DR PRIDE; P0A139; -.
DR GeneID; 66679376; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; MNQGEET; -.
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..166
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT /id="PRO_0000020127"
FT DOMAIN 54..166
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 166 AA; 17833 MW; 17353181435E5AC1 CRC64;
MEMLKFGKFA ALALAMAVAV GCSSKGGDNA GEGAAVDPNA GYGANTGAVD GSLSEEAALR
AITTFYFEYD SSDLKPEAMR ALDVHAKDLK ANGNRVVLEG NTDERGTREY NMALGERRAK
AVQRYLVLQG VSPAQLELVS YGEERPVATG NDEQSWAQNR RVELRK
