ID   Q44157_ACTPL            Unreviewed;       152 AA.
AC   Q44157;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000256|HAMAP-Rule:MF_02204};
DE            Short=PAL {ECO:0000256|HAMAP-Rule:MF_02204};
GN   Name=palA {ECO:0000313|EMBL:CAA61413.1};
GN   Synonyms=pal {ECO:0000256|HAMAP-Rule:MF_02204,
GN   ECO:0000313|EMBL:MCY6522950.1};
GN   ORFNames=NCTC10976_00323 {ECO:0000313|EMBL:VEJ16241.1}, OYG11_01605
GN   {ECO:0000313|EMBL:MCY6522950.1};
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715 {ECO:0000313|EMBL:CAA61413.1};
RN   [1] {ECO:0000313|EMBL:CAA61413.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8763621; DOI=10.1016/0923-2508(96)84710-3;
RA   Frey J., Kuhnert P., Villiger L., Nicolet J.;
RT   "Cloning and characterization of an Actinobacillus pleuropneumoniae outer
RT   membrane protein belonging to the family of PAL lipoproteins.";
RL   Res. Microbiol. 147:351-361(1996).
RN   [2] {ECO:0000313|EMBL:VEJ16241.1, ECO:0000313|Proteomes:UP000275510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10976 {ECO:0000313|EMBL:VEJ16241.1,
RC   ECO:0000313|Proteomes:UP000275510};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MCY6522950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=84/14 {ECO:0000313|EMBL:MCY6522950.1};
RX   PubMed=35051085;
RA   Byun J.W., Moon B.Y., Do K.H., Lee K., Lee H.Y., Kim W.I., So B., Lee W.K.;
RT   "O-Serogroups and Pathovirotypes of Escherichia coli Isolated from Post-
RT   Weaning Piglets Showing Diarrhoea and/or Oedema in South Korea.";
RL   Vet Sci 5 (2) 9:0-0(2021).
RN   [4] {ECO:0000313|EMBL:MCY6522950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=84/14 {ECO:0000313|EMBL:MCY6522950.1};
RA   Kardos G., Sarkozi R., Laczko L., Marton S., Makrai L., Banyai K.,
RA   Fodor L.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_02204}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02204}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02204}.
CC   -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000256|HAMAP-
CC       Rule:MF_02204}.
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DR   EMBL; X89009; CAA61413.1; -; Genomic_DNA.
DR   EMBL; JAPQFC010000001; MCY6522950.1; -; Genomic_DNA.
DR   EMBL; LR134515; VEJ16241.1; -; Genomic_DNA.
DR   RefSeq; WP_005596217.1; NZ_UIFY01000002.1.
DR   GeneID; 69417479; -.
DR   OMA; STESCWS; -.
DR   OrthoDB; 9809164at2; -.
DR   Proteomes; UP000275510; Chromosome 1.
DR   Proteomes; UP001077788; Unassembled WGS sequence.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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; OmpA-like domain; 1.
DR   HAMAP; MF_02204; Pal; 1.
DR   InterPro; IPR006664; OMP_bac.
DR   InterPro; IPR006665; OmpA-like.
DR   InterPro; IPR036737; OmpA-like_sf.
DR   InterPro; IPR039001; Pal.
DR   InterPro; IPR014169; Pal_lipo_C.
DR   NCBIfam; TIGR02802; Pal_lipo; 1.
DR   PANTHER; PTHR30329:SF22; PEPTIDOGLYCAN ASSOCIATED LIPOPROTEIN; 1.
DR   PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR   Pfam; PF00691; OmpA; 1.
DR   PRINTS; PR01021; OMPADOMAIN.
DR   SUPFAM; SSF103088; OmpA-like; 1.
DR   PROSITE; PS51123; OMPA_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02204};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02204}; Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_02204};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_02204};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02204};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02204};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02204}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..152
FT                   /note="Peptidoglycan-associated lipoprotein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039848352"
FT   DOMAIN          42..152
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51123"
SQ   SEQUENCE   152 AA;  16235 MW;  892C1E23E80406A7 CRC64;
     MKKLAKVLMI AAPAFVLAAC SSSSDNANAN ANANAGQFGG MTAEDLQTRY NTVYFGFDSY
     AVEGEYQQLL DAHAAYLTSA NGKVTVAGHA DERGTPEYNI ALGQRRADAV KNYLATKGAN
     QVSTVSYGEE KPAVLGHTEA DYAKNRRAVL EY
//